--- DOAJ_listed: '1' OA_place: publisher OA_type: gold PlanS_conform: '1' _id: '21369' 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.' 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. article_number: '1933' article_processing_charge: Yes article_type: original author: - first_name: Jing full_name: Hu, Jing last_name: Hu - first_name: Tom full_name: Scheidt, Tom last_name: Scheidt - first_name: Dev full_name: Thacker, Dev last_name: Thacker - first_name: Emil full_name: Axell, Emil last_name: Axell - first_name: Elin full_name: Stemme, Elin last_name: Stemme - first_name: Urszula full_name: Łapińska, Urszula last_name: Łapińska - first_name: Stefan full_name: Wennmalm, Stefan last_name: Wennmalm - first_name: Georg full_name: Meisl, Georg last_name: Meisl - first_name: Samo full_name: Curk, Samo id: 031eff0d-d481-11ee-8508-cd12a7a86e5b last_name: Curk orcid: 0000-0001-6160-9766 - first_name: Maria full_name: Andreasen, Maria last_name: Andreasen - first_name: Michele full_name: Vendruscolo, Michele last_name: Vendruscolo - first_name: Paolo full_name: Arosio, Paolo last_name: Arosio - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Jeremy D. full_name: Schmit, Jeremy D. last_name: Schmit - first_name: Tuomas P.J. full_name: Knowles, Tuomas P.J. last_name: Knowles - first_name: Emma full_name: Sparr, Emma last_name: Sparr - first_name: Sara full_name: Linse, Sara last_name: Linse - first_name: Thomas C.T. full_name: Michaels, Thomas C.T. last_name: Michaels - first_name: Alexander J. full_name: Dear, Alexander J. last_name: Dear citation: ama: Hu J, Scheidt T, Thacker D, et al. Structural defects in amyloid-β fibrils drive secondary nucleation. Nature Communications. 2026;17. doi:10.1038/s41467-026-69377-1 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. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-026-69377-1 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.” Nature Communications. Springer Nature, 2026. https://doi.org/10.1038/s41467-026-69377-1. ieee: J. Hu et al., “Structural defects in amyloid-β fibrils drive secondary nucleation,” Nature Communications, vol. 17. Springer Nature, 2026. 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. mla: Hu, Jing, et al. “Structural Defects in Amyloid-β Fibrils Drive Secondary Nucleation.” Nature Communications, vol. 17, 1933, Springer Nature, 2026, doi:10.1038/s41467-026-69377-1. 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). date_created: 2026-03-01T23:01:38Z date_published: 2026-02-20T00:00:00Z date_updated: 2026-03-02T09:36:48Z day: '20' ddc: - '570' department: - _id: AnSa doi: 10.1038/s41467-026-69377-1 ec_funded: 1 external_id: pmid: - '41708600' file: - access_level: open_access checksum: fa2b55b3a0d8978de7d2d061c7ad8779 content_type: application/pdf creator: dernst date_created: 2026-03-02T09:34:18Z date_updated: 2026-03-02T09:34:18Z file_id: '21377' file_name: 2026_NatureComm_Hu.pdf file_size: 4821073 relation: main_file success: 1 file_date_updated: 2026-03-02T09:34:18Z has_accepted_license: '1' intvolume: ' 17' language: - iso: eng month: '02' oa: 1 oa_version: Published Version pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: Nature Communications publication_identifier: eissn: - 2041-1723 publication_status: published publisher: Springer Nature quality_controlled: '1' scopus_import: '1' status: public title: Structural defects in amyloid-β fibrils drive secondary nucleation tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 17 year: '2026' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '21748' 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. 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. article_number: '144902' article_processing_charge: Yes (in subscription journal) article_type: original arxiv: 1 author: - first_name: Felix F full_name: Frey, Felix F id: a0270b37-8f1a-11ec-95c7-8e710c59a4f3 last_name: Frey orcid: 0000-0001-8501-6017 - first_name: Miguel full_name: Santana de Freitas Amaral, Miguel id: 4f2d02dd-47a9-11ec-ad10-82820ed3f501 last_name: Santana de Freitas Amaral - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 citation: ama: 'Frey FF, Santana de Freitas Amaral M, Šarić A. Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization. Journal of Chemical Physics. 2026;164(14). doi:10.1063/5.0325170' apa: 'Frey, F. F., 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. AIP Publishing. https://doi.org/10.1063/5.0325170' 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.” Journal of Chemical Physics. AIP Publishing, 2026. https://doi.org/10.1063/5.0325170.' 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,” Journal of Chemical Physics, vol. 164, no. 14. AIP Publishing, 2026.' 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.' mla: 'Frey, Felix F., et al. “Cracking Donuts and Sorting Lipids: Geometry Controls Archaeal Membrane Stability and Lipid Organization.” Journal of Chemical Physics, vol. 164, no. 14, 144902, AIP Publishing, 2026, doi:10.1063/5.0325170.' short: F.F. Frey, M. Santana de Freitas Amaral, A. Šarić, Journal of Chemical Physics 164 (2026). corr_author: '1' date_created: 2026-04-19T22:07:45Z date_published: 2026-04-14T00:00:00Z date_updated: 2026-05-05T12:40:41Z day: '14' ddc: - '540' department: - _id: AnSa doi: 10.1063/5.0325170 ec_funded: 1 external_id: arxiv: - '2603.15170' file: - access_level: open_access checksum: 2e10c4f4531676e0771ef3730e4b63a9 content_type: application/pdf creator: dernst date_created: 2026-05-05T12:35:24Z date_updated: 2026-05-05T12:35:24Z file_id: '21801' file_name: 2026_JourChemPhysics_Frey.pdf file_size: 8764791 relation: main_file success: 1 file_date_updated: 2026-05-05T12:35:24Z has_accepted_license: '1' intvolume: ' 164' issue: '14' language: - iso: eng month: '04' oa: 1 oa_version: Published Version project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: Journal of Chemical Physics publication_identifier: eissn: - 1089-7690 issn: - ' 0021-9606' publication_status: published publisher: AIP Publishing quality_controlled: '1' related_material: record: - id: '21800' relation: research_data status: public scopus_import: '1' status: public title: 'Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization' tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 164 year: '2026' ... --- OA_place: publisher OA_type: hybrid _id: '20318' abstract: - lang: eng 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. 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. article_processing_charge: Yes (via OA deal) article_type: original arxiv: 1 author: - first_name: Maitane full_name: Muñoz Basagoiti, Maitane id: 1a8a7950-82cd-11ed-bd4f-9624c913a607 last_name: Muñoz Basagoiti orcid: 0000-0003-1483-1457 - first_name: Felix F full_name: Frey, Felix F id: a0270b37-8f1a-11ec-95c7-8e710c59a4f3 last_name: Frey orcid: 0000-0001-8501-6017 - first_name: Billie full_name: Meadowcroft, Billie id: a4725fd6-932b-11ed-81e2-c098c7f37ae1 last_name: Meadowcroft orcid: 0000-0003-3441-1337 - first_name: Miguel full_name: Santana de Freitas Amaral, Miguel id: 4f2d02dd-47a9-11ec-ad10-82820ed3f501 last_name: Santana de Freitas Amaral - first_name: Adam full_name: Prada, Adam id: a43ed60a-dd22-11ed-9bf7-b34133792ea9 last_name: Prada - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 citation: 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. Soft Matter. 2025;21(40):7736-7756. doi:10.1039/d5sm00148j' apa: 'Muñoz Basagoiti, M., Frey, F. F., 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. Royal Society of Chemistry. https://doi.org/10.1039/d5sm00148j' 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.” Soft Matter. Royal Society of Chemistry, 2025. https://doi.org/10.1039/d5sm00148j.' 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,” Soft Matter, vol. 21, no. 40. Royal Society of Chemistry, pp. 7736–7756, 2025.' 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.' mla: 'Muñoz Basagoiti, Maitane, et al. “A Tutorial for Mesoscale Computer Simulations of Lipid Membranes: Tether Pulling, Tubulation and Fluctuations.” Soft Matter, vol. 21, no. 40, Royal Society of Chemistry, 2025, pp. 7736–56, doi:10.1039/d5sm00148j.' short: M. Muñoz Basagoiti, F.F. Frey, B. Meadowcroft, M. Santana de Freitas Amaral, A. Prada, A. Šarić, Soft Matter 21 (2025) 7736–7756. corr_author: '1' date_created: 2025-09-10T05:34:36Z date_published: 2025-07-28T00:00:00Z date_updated: 2025-12-30T10:16:52Z day: '28' ddc: - '540' department: - _id: AnSa doi: 10.1039/d5sm00148j ec_funded: 1 external_id: arxiv: - '2502.09798' isi: - '001562846800001' file: - access_level: open_access checksum: 590bedad19b6f6d40a7ee036a056a6d9 content_type: application/pdf creator: dernst date_created: 2025-12-30T10:16:40Z date_updated: 2025-12-30T10:16:40Z file_id: '20912' file_name: 2025_SoftMatter_MunozBasagoiti.pdf file_size: 4841140 relation: main_file success: 1 file_date_updated: 2025-12-30T10:16:40Z has_accepted_license: '1' intvolume: ' 21' isi: 1 issue: '40' language: - iso: eng month: '07' oa: 1 oa_version: Published Version page: 7736-7756 project: - _id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c call_identifier: H2020 grant_number: '101034413' name: 'IST-BRIDGE: International postdoctoral program' - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' - _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 publication_identifier: eissn: - 1744-6848 issn: - 1744-683X publication_status: published publisher: Royal Society of Chemistry quality_controlled: '1' scopus_import: '1' status: public title: 'A tutorial for mesoscale computer simulations of lipid membranes: Tether pulling, tubulation and fluctuations' tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 21 year: '2025' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '20530' abstract: - lang: eng 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. 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. article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Joe full_name: Parham, Joe last_name: Parham - first_name: Valerio full_name: Sorichetti, Valerio id: ef8a92cb-c7b6-11ec-8bea-e1fd5847bc5b last_name: Sorichetti orcid: 0000-0002-9645-6576 - first_name: Alice full_name: Cezanne, Alice last_name: Cezanne - first_name: Sherman full_name: Foo, Sherman last_name: Foo - first_name: Yin Wei full_name: Kuo, Yin Wei last_name: Kuo - first_name: Baukje full_name: Hoogenberg, Baukje last_name: Hoogenberg - first_name: Arthur full_name: Radoux-Mergault, Arthur last_name: Radoux-Mergault - first_name: Eloise full_name: Mawdesley, Eloise last_name: Mawdesley - first_name: Lydia Daniels full_name: Gatward, Lydia Daniels last_name: Gatward - first_name: Jerome full_name: Boulanger, Jerome last_name: Boulanger - first_name: Ulrike full_name: Schulze, Ulrike last_name: Schulze - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Buzz full_name: Baum, Buzz last_name: Baum citation: ama: Parham J, Sorichetti V, Cezanne A, et al. Temporal and spatial coordination of DNA segregation and cell division in an archaeon. Proceedings of the National Academy of Sciences. 2025;122(42):e2513939122. doi:10.1073/pnas.2513939122 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. Proceedings of the National Academy of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.2513939122 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.” Proceedings of the National Academy of Sciences. National Academy of Sciences, 2025. https://doi.org/10.1073/pnas.2513939122. ieee: J. Parham et al., “Temporal and spatial coordination of DNA segregation and cell division in an archaeon,” Proceedings of the National Academy of Sciences, 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. mla: Parham, Joe, et al. “Temporal and Spatial Coordination of DNA Segregation and Cell Division in an Archaeon.” Proceedings of the National Academy of Sciences, vol. 122, no. 42, National Academy of Sciences, 2025, p. e2513939122, doi:10.1073/pnas.2513939122. 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. date_created: 2025-10-26T23:01:33Z date_published: 2025-10-21T00:00:00Z date_updated: 2026-02-16T12:32:31Z day: '21' ddc: - '570' department: - _id: AnSa doi: 10.1073/pnas.2513939122 ec_funded: 1 external_id: isi: - '001620648600001' pmid: - '41091768' file: - access_level: open_access checksum: 3555d51f438d2e356039a9b697eac3ee content_type: application/pdf creator: dernst date_created: 2025-10-27T08:12:59Z date_updated: 2025-10-27T08:12:59Z file_id: '20543' file_name: 2025_PNAS_Parham.pdf file_size: 2649194 relation: main_file success: 1 file_date_updated: 2025-10-27T08:12:59Z has_accepted_license: '1' intvolume: ' 122' isi: 1 issue: '42' language: - iso: eng month: '10' oa: 1 oa_version: Published Version page: e2513939122 pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' - _id: 349b6ff1-11ca-11ed-8bc3-f006047c2eeb name: EMBO Young Investigator Program - Andela Saric publication: Proceedings of the National Academy of Sciences publication_identifier: eissn: - 1091-6490 publication_status: published publisher: National Academy of Sciences quality_controlled: '1' scopus_import: '1' status: public title: Temporal and spatial coordination of DNA segregation and cell division in an archaeon tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 122 year: '2025' ... --- DOAJ_listed: '1' OA_place: publisher OA_type: gold PlanS_conform: '1' _id: '21235' abstract: - lang: eng 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. 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.)." article_number: '033010' article_processing_charge: Yes article_type: original author: - first_name: Valerio full_name: Sorichetti, Valerio id: ef8a92cb-c7b6-11ec-8bea-e1fd5847bc5b last_name: Sorichetti orcid: 0000-0002-9645-6576 - first_name: Paul full_name: Robin, Paul id: 48c58128-57b0-11ee-9095-dc28fd97fc1d last_name: Robin orcid: 0000-0002-5728-9189 - first_name: Ivan full_name: Palaia, Ivan id: 9c805cd2-4b75-11ec-a374-db6dd0ed57fa last_name: Palaia orcid: ' 0000-0002-8843-9485 ' - first_name: Alberto full_name: Hernandez-Armendariz, Alberto last_name: Hernandez-Armendariz - first_name: Sara full_name: Cuylen-Haering, Sara last_name: Cuylen-Haering - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 citation: ama: Sorichetti V, Robin P, Palaia I, Hernandez-Armendariz A, Cuylen-Haering S, Šarić A. Charge distribution of the coating brush drives interchromosome attraction. PRX Life. 2025;3(3). doi:10.1103/41fd-r847 apa: 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. American Physical Society. https://doi.org/10.1103/41fd-r847 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.” PRX Life. American Physical Society, 2025. https://doi.org/10.1103/41fd-r847. 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,” PRX Life, vol. 3, no. 3. American Physical Society, 2025. 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.” PRX Life, vol. 3, no. 3, 033010, American Physical Society, 2025, doi:10.1103/41fd-r847. short: V. Sorichetti, P. Robin, I. Palaia, A. Hernandez-Armendariz, S. Cuylen-Haering, A. Šarić, PRX Life 3 (2025). corr_author: '1' date_created: 2026-02-16T14:50:32Z date_published: 2025-08-11T00:00:00Z date_updated: 2026-02-17T11:16:26Z day: '11' ddc: - '570' department: - _id: AnSa - _id: EdHa doi: 10.1103/41fd-r847 ec_funded: 1 file: - access_level: open_access checksum: 1702b9bdbfd902a7c08aa4f1479b390d content_type: application/pdf creator: dernst date_created: 2026-02-17T11:12:30Z date_updated: 2026-02-17T11:12:30Z file_id: '21287' file_name: 2025_PRXLife_Sorichetti.pdf file_size: 3732843 relation: main_file success: 1 file_date_updated: 2026-02-17T11:12:30Z has_accepted_license: '1' intvolume: ' 3' issue: '3' language: - iso: eng month: '08' oa: 1 oa_version: Published Version project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' - _id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c call_identifier: H2020 grant_number: '101034413' name: 'IST-BRIDGE: International postdoctoral program' - _id: 349b6ff1-11ca-11ed-8bc3-f006047c2eeb name: EMBO Young Investigator Program - Andela Saric publication: PRX Life publication_identifier: eissn: - 2835-8279 publication_status: published publisher: American Physical Society quality_controlled: '1' status: public title: Charge distribution of the coating brush drives interchromosome attraction tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 3 year: '2025' ... --- DOAJ_listed: '1' OA_place: publisher OA_type: gold PlanS_conform: '1' _id: '21251' abstract: - lang: eng 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. 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. article_number: '105432' article_processing_charge: Yes article_type: original author: - first_name: Miguel full_name: Santana de Freitas Amaral, Miguel id: 4f2d02dd-47a9-11ec-ad10-82820ed3f501 last_name: Santana de Freitas Amaral - first_name: Felix F full_name: Frey, Felix F id: a0270b37-8f1a-11ec-95c7-8e710c59a4f3 last_name: Frey orcid: 0000-0001-8501-6017 - first_name: Xiuyun full_name: Jiang, Xiuyun last_name: Jiang - first_name: Buzz full_name: Baum, Buzz last_name: Baum - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 citation: ama: Santana de Freitas Amaral M, Frey FF, Jiang X, Baum B, Šarić A. Balancing stability and flexibility when reshaping archaeal membranes. eLife. 2025;14. doi:10.7554/elife.105432 apa: Santana de Freitas Amaral, M., Frey, F. F., Jiang, X., Baum, B., & Šarić, A. (2025). Balancing stability and flexibility when reshaping archaeal membranes. ELife. eLife Sciences Publications. https://doi.org/10.7554/elife.105432 chicago: Santana de Freitas Amaral, Miguel, Felix F Frey, Xiuyun Jiang, Buzz Baum, and Anđela Šarić. “Balancing Stability and Flexibility When Reshaping Archaeal Membranes.” ELife. eLife Sciences Publications, 2025. https://doi.org/10.7554/elife.105432. ieee: M. Santana de Freitas Amaral, F. F. Frey, X. Jiang, B. Baum, and A. Šarić, “Balancing stability and flexibility when reshaping archaeal membranes,” eLife, vol. 14. eLife Sciences Publications, 2025. 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.” ELife, vol. 14, 105432, eLife Sciences Publications, 2025, doi:10.7554/elife.105432. short: M. Santana de Freitas Amaral, F.F. Frey, X. Jiang, B. Baum, A. Šarić, ELife 14 (2025). corr_author: '1' date_created: 2026-02-16T15:43:57Z date_published: 2025-10-07T00:00:00Z date_updated: 2026-02-23T11:49:05Z day: '07' ddc: - '570' department: - _id: AnSa doi: 10.7554/elife.105432 ec_funded: 1 external_id: pmid: - '41056191 ' file: - access_level: open_access checksum: 4116cd5143558ded995fb9ff5fcbc7e0 content_type: application/pdf creator: dernst date_created: 2026-02-17T13:02:02Z date_updated: 2026-02-17T13:02:02Z file_id: '21305' file_name: 2025_elife_Amaral.pdf file_size: 10668225 relation: main_file success: 1 file_date_updated: 2026-02-17T13:02:02Z has_accepted_license: '1' intvolume: ' 14' language: - iso: eng month: '10' oa: 1 oa_version: Published Version pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: eLife publication_identifier: eissn: - 2050-084X publication_status: published publisher: eLife Sciences Publications quality_controlled: '1' related_material: record: - id: '21304' relation: software status: public status: public title: Balancing stability and flexibility when reshaping archaeal membranes tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 14 year: '2025' ... --- DOAJ_listed: '1' OA_place: publisher OA_type: gold PlanS_conform: '1' _id: '21256' 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. 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.). article_number: '033019' article_processing_charge: Yes article_type: original author: - first_name: Billie full_name: Meadowcroft, Billie id: a4725fd6-932b-11ed-81e2-c098c7f37ae1 last_name: Meadowcroft orcid: 0000-0003-3441-1337 - first_name: Valerio full_name: Sorichetti, Valerio id: ef8a92cb-c7b6-11ec-8bea-e1fd5847bc5b last_name: Sorichetti orcid: 0000-0002-9645-6576 - first_name: Eryk full_name: Ratajczyk, Eryk last_name: Ratajczyk - first_name: Fernanda L full_name: Perez Verdugo, Fernanda L id: 4ecec223-9070-11ef-a0a9-bc76077bea8d last_name: Perez Verdugo - first_name: Nargess full_name: Khalilgharibi, Nargess last_name: Khalilgharibi - first_name: Yanlan full_name: Mao, Yanlan last_name: Mao - first_name: Ivan full_name: Palaia, Ivan id: 9c805cd2-4b75-11ec-a374-db6dd0ed57fa last_name: Palaia orcid: ' 0000-0002-8843-9485 ' - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 citation: ama: Meadowcroft B, Sorichetti V, Ratajczyk E, et al. Nonequilibrium remodeling of collagen IV networks in Silico. PRX Life. 2025;3. doi:10.1103/gdd5-rnh7 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. PRX Life. American Physical Society. https://doi.org/10.1103/gdd5-rnh7 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.” PRX Life. American Physical Society, 2025. https://doi.org/10.1103/gdd5-rnh7. ieee: B. Meadowcroft et al., “Nonequilibrium remodeling of collagen IV networks in Silico,” PRX Life, vol. 3. American Physical Society, 2025. 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. mla: Meadowcroft, Billie, et al. “Nonequilibrium Remodeling of Collagen IV Networks in Silico.” PRX Life, vol. 3, 033019, American Physical Society, 2025, doi:10.1103/gdd5-rnh7. short: B. Meadowcroft, V. Sorichetti, E. Ratajczyk, F.L. Perez Verdugo, N. Khalilgharibi, Y. Mao, I. Palaia, A. Šarić, PRX Life 3 (2025). corr_author: '1' date_created: 2026-02-16T15:55:03Z date_published: 2025-09-05T00:00:00Z date_updated: 2026-02-17T13:37:38Z day: '05' ddc: - '570' department: - _id: AnSa doi: 10.1103/gdd5-rnh7 ec_funded: 1 file: - access_level: open_access checksum: 04cae5231d97e533145c493880fadbd9 content_type: application/pdf creator: dernst date_created: 2026-02-17T13:36:01Z date_updated: 2026-02-17T13:36:01Z file_id: '21308' file_name: 2025_PRXLife_Meadowcroft.pdf file_size: 2277704 relation: main_file success: 1 file_date_updated: 2026-02-17T13:36:01Z has_accepted_license: '1' intvolume: ' 3' language: - iso: eng month: '09' oa: 1 oa_version: Published Version project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' - _id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c call_identifier: H2020 grant_number: '101034413' name: 'IST-BRIDGE: International postdoctoral program' - _id: 349b6ff1-11ca-11ed-8bc3-f006047c2eeb name: EMBO Young Investigator Program - Andela Saric publication: PRX Life publication_identifier: eissn: - 2835-8279 publication_status: published publisher: American Physical Society quality_controlled: '1' status: public title: Nonequilibrium remodeling of collagen IV networks in Silico tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 3 year: '2025' ... --- _id: '18072' 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. 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). article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Alberto full_name: Hernandez-Armendariz, Alberto last_name: Hernandez-Armendariz - first_name: Valerio full_name: Sorichetti, Valerio id: ef8a92cb-c7b6-11ec-8bea-e1fd5847bc5b last_name: Sorichetti orcid: 0000-0002-9645-6576 - first_name: Yuki full_name: Hayashi, Yuki last_name: Hayashi - first_name: Zuzana full_name: Koskova, Zuzana last_name: Koskova - first_name: Andreas full_name: Brunner, Andreas last_name: Brunner - first_name: Jan full_name: Ellenberg, Jan last_name: Ellenberg - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Sara full_name: Cuylen-Haering, Sara last_name: Cuylen-Haering citation: ama: Hernandez-Armendariz A, Sorichetti V, Hayashi Y, et al. A liquid-like coat mediates chromosome clustering during mitotic exit. Molecular Cell. 2024;84(17):P3254-3270.E9. doi:10.1016/j.molcel.2024.07.022 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. Molecular Cell. Cell Press. https://doi.org/10.1016/j.molcel.2024.07.022 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.” Molecular Cell. Cell Press, 2024. https://doi.org/10.1016/j.molcel.2024.07.022. ieee: A. Hernandez-Armendariz et al., “A liquid-like coat mediates chromosome clustering during mitotic exit,” Molecular Cell, vol. 84, no. 17. Cell Press, p. P3254–3270.E9, 2024. 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. mla: Hernandez-Armendariz, Alberto, et al. “A Liquid-like Coat Mediates Chromosome Clustering during Mitotic Exit.” Molecular Cell, vol. 84, no. 17, Cell Press, 2024, p. P3254–3270.E9, doi:10.1016/j.molcel.2024.07.022. 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. date_created: 2024-09-15T22:01:41Z date_published: 2024-09-05T00:00:00Z date_updated: 2025-09-08T09:23:02Z day: '05' ddc: - '570' department: - _id: AnSa doi: 10.1016/j.molcel.2024.07.022 ec_funded: 1 external_id: isi: - '001309051100001' pmid: - '39153474' file: - access_level: open_access checksum: 3f360e0287b8ec79fb2b8b02b5070360 content_type: application/pdf creator: dernst date_created: 2024-09-16T07:38:38Z date_updated: 2024-09-16T07:38:38Z file_id: '18075' file_name: 2024_MolecularCell_HernandezArmendariz.pdf file_size: 11654644 relation: main_file success: 1 file_date_updated: 2024-09-16T07:38:38Z has_accepted_license: '1' intvolume: ' 84' isi: 1 issue: '17' language: - iso: eng month: '09' oa: 1 oa_version: Published Version page: P3254-3270.E9 pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: Molecular Cell publication_identifier: eissn: - 1097-4164 issn: - 1097-2765 publication_status: published publisher: Cell Press quality_controlled: '1' scopus_import: '1' status: public title: A liquid-like coat mediates chromosome clustering during mitotic exit tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 84 year: '2024' ... --- OA_place: publisher OA_type: hybrid _id: '18526' 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. 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. article_number: e2409407121 article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Ethan full_name: Weiner, Ethan last_name: Weiner - first_name: Elizabeth full_name: Berryman, Elizabeth last_name: Berryman - first_name: Felix F full_name: Frey, Felix F id: a0270b37-8f1a-11ec-95c7-8e710c59a4f3 last_name: Frey orcid: 0000-0001-8501-6017 - first_name: Ariadna González full_name: Solís, Ariadna González last_name: Solís - first_name: André full_name: Leier, André last_name: Leier - first_name: Tatiana Marquez full_name: Lago, Tatiana Marquez last_name: Lago - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Marisa S. full_name: Otegui, Marisa S. last_name: Otegui citation: ama: Weiner E, Berryman E, Frey FF, et al. Endosomal membrane budding patterns in plants. Proceedings of the National Academy of Sciences of the United States of America. 2024;121(44). doi:10.1073/pnas.2409407121 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. Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences. https://doi.org/10.1073/pnas.2409407121 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.” Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 2024. https://doi.org/10.1073/pnas.2409407121. ieee: E. Weiner et al., “Endosomal membrane budding patterns in plants,” Proceedings of the National Academy of Sciences of the United States of America, vol. 121, no. 44. National Academy of Sciences, 2024. 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. mla: Weiner, Ethan, et al. “Endosomal Membrane Budding Patterns in Plants.” Proceedings of the National Academy of Sciences of the United States of America, vol. 121, no. 44, e2409407121, National Academy of Sciences, 2024, doi:10.1073/pnas.2409407121. 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). date_created: 2024-11-10T23:01:59Z date_published: 2024-10-29T00:00:00Z date_updated: 2025-09-08T14:38:35Z day: '29' ddc: - '570' department: - _id: AnSa doi: 10.1073/pnas.2409407121 ec_funded: 1 external_id: isi: - '001349500800007' pmid: - '39441629' file: - access_level: open_access checksum: 21c82d2ab58ff99b2bd0489797be42e5 content_type: application/pdf creator: dernst date_created: 2024-11-11T09:35:15Z date_updated: 2024-11-11T09:35:15Z file_id: '18538' file_name: 2024_PNAS_Weiner.pdf file_size: 5268074 relation: main_file success: 1 file_date_updated: 2024-11-11T09:35:15Z has_accepted_license: '1' intvolume: ' 121' isi: 1 issue: '44' language: - iso: eng license: https://creativecommons.org/licenses/by-nc-nd/4.0/ month: '10' oa: 1 oa_version: Published Version pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: Proceedings of the National Academy of Sciences of the United States of America publication_identifier: eissn: - 1091-6490 issn: - 0027-8424 publication_status: published publisher: National Academy of Sciences quality_controlled: '1' scopus_import: '1' status: public title: Endosomal membrane budding patterns in plants tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 121 year: '2024' ... --- _id: '14844' abstract: - lang: eng 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.' 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). article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Ali full_name: Azadbakht, Ali last_name: Azadbakht - first_name: Billie full_name: Meadowcroft, Billie id: a4725fd6-932b-11ed-81e2-c098c7f37ae1 last_name: Meadowcroft orcid: 0000-0003-3441-1337 - first_name: Juraj full_name: Majek, Juraj id: 3e6d9473-f38e-11ec-8ae0-c4e05a8aa9e1 last_name: Majek - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Daniela J. full_name: Kraft, Daniela J. last_name: Kraft citation: ama: Azadbakht A, Meadowcroft B, Majek J, Šarić A, Kraft DJ. Nonadditivity in interactions between three membrane-wrapped colloidal spheres. Biophysical Journal. 2024;123(3):307-316. doi:10.1016/j.bpj.2023.12.020 apa: Azadbakht, A., Meadowcroft, B., Majek, J., Šarić, A., & Kraft, D. J. (2024). Nonadditivity in interactions between three membrane-wrapped colloidal spheres. Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2023.12.020 chicago: Azadbakht, Ali, Billie Meadowcroft, Juraj Majek, Anđela Šarić, and Daniela J. Kraft. “Nonadditivity in Interactions between Three Membrane-Wrapped Colloidal Spheres.” Biophysical Journal. Elsevier, 2024. https://doi.org/10.1016/j.bpj.2023.12.020. ieee: A. Azadbakht, B. Meadowcroft, J. Majek, A. Šarić, and D. J. Kraft, “Nonadditivity in interactions between three membrane-wrapped colloidal spheres,” Biophysical Journal, vol. 123, no. 3. Elsevier, pp. 307–316, 2024. 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. mla: Azadbakht, Ali, et al. “Nonadditivity in Interactions between Three Membrane-Wrapped Colloidal Spheres.” Biophysical Journal, vol. 123, no. 3, Elsevier, 2024, pp. 307–16, doi:10.1016/j.bpj.2023.12.020. short: A. Azadbakht, B. Meadowcroft, J. Majek, A. Šarić, D.J. Kraft, Biophysical Journal 123 (2024) 307–316. date_created: 2024-01-21T23:00:56Z date_published: 2024-02-06T00:00:00Z date_updated: 2025-09-04T11:46:15Z day: '06' ddc: - '570' department: - _id: AnSa doi: 10.1016/j.bpj.2023.12.020 ec_funded: 1 external_id: isi: - '001185235900001' pmid: - '38158654' file: - access_level: open_access checksum: 1c8fe1cf950394875b65b90da86428ff content_type: application/pdf creator: dernst date_created: 2024-07-16T12:09:55Z date_updated: 2024-07-16T12:09:55Z file_id: '17266' file_name: 2024_BiophysicalJournal_Azadbakht.pdf file_size: 3189926 relation: main_file success: 1 file_date_updated: 2024-07-16T12:09:55Z has_accepted_license: '1' intvolume: ' 123' isi: 1 issue: '3' language: - iso: eng month: '02' oa: 1 oa_version: Published Version page: 307-316 pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: Biophysical Journal publication_identifier: eissn: - 1542-0086 issn: - 0006-3495 publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: Nonadditivity in interactions between three membrane-wrapped colloidal spheres tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 123 year: '2024' ... --- APC_amount: 5936,71 EUR OA_place: publisher OA_type: hybrid _id: '15001' abstract: - lang: eng 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." 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.). article_number: e2220075121 article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Samo full_name: Curk, Samo id: 031eff0d-d481-11ee-8508-cd12a7a86e5b last_name: Curk orcid: 0000-0001-6160-9766 - first_name: Johannes full_name: Krausser, Johannes last_name: Krausser - first_name: Georg full_name: Meisl, Georg last_name: Meisl - first_name: Daan full_name: Frenkel, Daan last_name: Frenkel - first_name: Sara full_name: Linse, Sara last_name: Linse - first_name: Thomas C.T. full_name: Michaels, Thomas C.T. last_name: Michaels - first_name: Tuomas P.J. full_name: Knowles, Tuomas P.J. last_name: Knowles - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 citation: ama: Curk S, Krausser J, Meisl G, et al. 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. 2024;121(7). doi:10.1073/pnas.2220075121 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. Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences. https://doi.org/10.1073/pnas.2220075121 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.” Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 2024. https://doi.org/10.1073/pnas.2220075121. ieee: S. Curk et al., “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, vol. 121, no. 7. National Academy of Sciences, 2024. 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. mla: Curk, Samo, et al. “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, vol. 121, no. 7, e2220075121, National Academy of Sciences, 2024, doi:10.1073/pnas.2220075121. 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). corr_author: '1' date_created: 2024-02-18T23:01:00Z date_published: 2024-02-13T00:00:00Z date_updated: 2025-09-04T12:03:12Z day: '13' ddc: - '570' department: - _id: AnSa doi: 10.1073/pnas.2220075121 ec_funded: 1 external_id: isi: - '001169063600007' pmid: - '38335256' file: - access_level: open_access checksum: 5aeb65bcc0dd829b1f9ab307c5031d4b content_type: application/pdf creator: dernst date_created: 2024-02-26T08:20:00Z date_updated: 2024-02-26T08:20:00Z file_id: '15026' file_name: 2024_PNAS_Curk.pdf file_size: 7699487 relation: main_file success: 1 file_date_updated: 2024-02-26T08:20:00Z has_accepted_license: '1' intvolume: ' 121' isi: 1 issue: '7' language: - iso: eng month: '02' oa: 1 oa_version: Published Version pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: Proceedings of the National Academy of Sciences of the United States of America publication_identifier: eissn: - 1091-6490 publication_status: published publisher: National Academy of Sciences quality_controlled: '1' related_material: record: - id: '15027' relation: research_data status: public scopus_import: '1' status: public title: Self-replication of Aβ42 aggregates occurs on small and isolated fibril sites tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 121 year: '2024' ... --- OA_place: publisher OA_type: hybrid _id: '17239' 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. 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). article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Clara full_name: Garcia-Sacristan, Clara last_name: Garcia-Sacristan - first_name: Victor G. full_name: Gisbert, Victor G. last_name: Gisbert - first_name: Kevin full_name: Klein, Kevin id: 1e7ede04-9e54-11f0-9ec4-8d4d5563c398 last_name: Klein - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Ricardo full_name: Garcia, Ricardo last_name: Garcia citation: ama: Garcia-Sacristan C, Gisbert VG, Klein K, Šarić A, Garcia R. In operando imaging electrostatic-driven disassembly and reassembly of collagen nanostructures. ACS Nano. 2024;18(28):18485-18492. doi:10.1021/acsnano.4c03839 apa: Garcia-Sacristan, C., Gisbert, V. G., Klein, K., Šarić, A., & Garcia, R. (2024). In operando imaging electrostatic-driven disassembly and reassembly of collagen nanostructures. ACS Nano. American Chemical Society. https://doi.org/10.1021/acsnano.4c03839 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.” ACS Nano. American Chemical Society, 2024. https://doi.org/10.1021/acsnano.4c03839. 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,” ACS Nano, 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. mla: Garcia-Sacristan, Clara, et al. “In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures.” ACS Nano, vol. 18, no. 28, American Chemical Society, 2024, pp. 18485–92, doi:10.1021/acsnano.4c03839. short: C. Garcia-Sacristan, V.G. Gisbert, K. Klein, A. Šarić, R. Garcia, ACS Nano 18 (2024) 18485–18492. date_created: 2024-07-14T22:01:12Z date_published: 2024-07-16T00:00:00Z date_updated: 2025-12-16T09:01:10Z day: '16' ddc: - '540' department: - _id: AnSa doi: 10.1021/acsnano.4c03839 ec_funded: 1 external_id: isi: - '001263155500001' pmid: - '38958189' file: - access_level: open_access checksum: b7e9ce718e92f568bcb3810e8e28e458 content_type: application/pdf creator: dernst date_created: 2025-01-09T12:06:48Z date_updated: 2025-01-09T12:06:48Z file_id: '18808' file_name: 2024_ACSNano_GarciaSacristan.pdf file_size: 10036838 relation: main_file success: 1 file_date_updated: 2025-01-09T12:06:48Z has_accepted_license: '1' intvolume: ' 18' isi: 1 issue: '28' language: - iso: eng month: '07' oa: 1 oa_version: Published Version page: 18485-18492 pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: ACS Nano publication_identifier: eissn: - 1936-086X issn: - 1936-0851 publication_status: published publisher: American Chemical Society quality_controlled: '1' scopus_import: '1' status: public title: In operando imaging electrostatic-driven disassembly and reassembly of collagen nanostructures tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 18 year: '2024' ... --- APC_amount: 12348 EUR OA_place: publisher OA_type: hybrid _id: '17460' 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. 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.). article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Christian Eduardo full_name: Vanhille-Campos, Christian Eduardo id: 3adeca52-9313-11ed-b1ac-c170b2505714 last_name: Vanhille-Campos - first_name: Kevin D. full_name: Whitley, Kevin D. last_name: Whitley - first_name: Philipp full_name: Radler, Philipp id: 40136C2A-F248-11E8-B48F-1D18A9856A87 last_name: Radler orcid: '0000-0001-9198-2182 ' - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 - first_name: Séamus full_name: Holden, Séamus last_name: Holden - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 citation: 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. Nature Physics. 2024;20:1670-1678. doi:10.1038/s41567-024-02597-8 apa: Vanhille-Campos, C. E., Whitley, K. D., Radler, P., Loose, M., Holden, S., & Šarić, A. (2024). Self-organization of mortal filaments and its role in bacterial division ring formation. Nature Physics. Springer Nature. https://doi.org/10.1038/s41567-024-02597-8 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.” Nature Physics. Springer Nature, 2024. https://doi.org/10.1038/s41567-024-02597-8. 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,” Nature Physics, vol. 20. Springer Nature, pp. 1670–1678, 2024. 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. mla: Vanhille-Campos, Christian Eduardo, et al. “Self-Organization of Mortal Filaments and Its Role in Bacterial Division Ring Formation.” Nature Physics, vol. 20, Springer Nature, 2024, pp. 1670–78, doi:10.1038/s41567-024-02597-8. short: C.E. Vanhille-Campos, K.D. Whitley, P. Radler, M. Loose, S. Holden, A. Šarić, Nature Physics 20 (2024) 1670–1678. corr_author: '1' date_created: 2024-08-25T22:01:08Z date_published: 2024-10-01T00:00:00Z date_updated: 2025-09-08T09:02:20Z day: '01' ddc: - '570' department: - _id: AnSa - _id: MaLo doi: 10.1038/s41567-024-02597-8 ec_funded: 1 external_id: isi: - '001289394500005' pmid: - '39416851' file: - access_level: open_access checksum: c4842152e2b90d67f48ea8c9ed7c473b content_type: application/pdf creator: dernst date_created: 2025-04-14T06:06:35Z date_updated: 2025-04-14T06:06:35Z file_id: '19556' file_name: 2024_NaturePhysics_VanhilleCampos.pdf file_size: 8058249 relation: main_file success: 1 file_date_updated: 2025-04-14T06:06:35Z has_accepted_license: '1' intvolume: ' 20' isi: 1 language: - iso: eng month: '10' oa: 1 oa_version: Published Version page: 1670-1678 pmid: 1 project: - _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d grant_number: P34607 name: In vitro reconstitution of bacterial cell division - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: Nature Physics publication_identifier: eissn: - 1745-2481 issn: - 1745-2473 publication_status: published publisher: Springer Nature quality_controlled: '1' scopus_import: '1' status: public title: Self-organization of mortal filaments and its role in bacterial division ring formation tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 20 year: '2024' ... --- OA_place: repository _id: '18670' abstract: - lang: eng 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. 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." article_processing_charge: No author: - first_name: Miguel full_name: Santana de Freitas Amaral, Miguel id: 4f2d02dd-47a9-11ec-ad10-82820ed3f501 last_name: Santana de Freitas Amaral - first_name: Felix F full_name: Frey, Felix F id: a0270b37-8f1a-11ec-95c7-8e710c59a4f3 last_name: Frey orcid: 0000-0001-8501-6017 - first_name: Xiuyun full_name: Jiang, Xiuyun last_name: Jiang - first_name: Buzz full_name: Baum, Buzz last_name: Baum - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 citation: ama: 'Santana de Freitas Amaral M, Frey FF, Jiang X, Baum B, Šarić A. Stability vs flexibility: Reshaping archaeal membranes in silico. bioRxiv. doi:10.1101/2024.10.18.619072' apa: 'Santana de Freitas Amaral, M., Frey, F. F., Jiang, X., Baum, B., & Šarić, A. (n.d.). Stability vs flexibility: Reshaping archaeal membranes in silico. bioRxiv. https://doi.org/10.1101/2024.10.18.619072' chicago: 'Santana de Freitas Amaral, Miguel, Felix F Frey, Xiuyun Jiang, Buzz Baum, and Anđela Šarić. “Stability vs Flexibility: Reshaping Archaeal Membranes in Silico.” BioRxiv, n.d. https://doi.org/10.1101/2024.10.18.619072.' ieee: 'M. Santana de Freitas Amaral, F. F. Frey, X. Jiang, B. Baum, and A. Šarić, “Stability vs flexibility: Reshaping archaeal membranes in silico,” bioRxiv. .' ista: 'Santana de Freitas Amaral M, Frey FF, Jiang X, Baum B, Šarić A. Stability vs flexibility: Reshaping archaeal membranes in silico. bioRxiv, 10.1101/2024.10.18.619072.' mla: 'Santana de Freitas Amaral, Miguel, et al. “Stability vs Flexibility: Reshaping Archaeal Membranes in Silico.” BioRxiv, doi:10.1101/2024.10.18.619072.' short: M. Santana de Freitas Amaral, F.F. Frey, X. Jiang, B. Baum, A. Šarić, BioRxiv (n.d.). corr_author: '1' date_created: 2024-12-18T10:07:45Z date_published: 2024-11-27T00:00:00Z date_updated: 2026-06-15T22:30:28Z day: '27' department: - _id: AnSa doi: 10.1101/2024.10.18.619072 ec_funded: 1 language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1101/2024.10.18.619072 month: '11' oa: 1 oa_version: Preprint project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: bioRxiv publication_status: draft related_material: record: - id: '18661' relation: dissertation_contains status: public status: public title: 'Stability vs flexibility: Reshaping archaeal membranes in silico' tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: preprint user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 year: '2024' ... --- _id: '13971' abstract: - lang: eng text: When in equilibrium, thermal forces agitate molecules, which then diffuse, collide and bind to form materials. However, the space of accessible structures in which micron-scale particles can be organized by thermal forces is limited, owing to the slow dynamics and metastable states. Active agents in a passive fluid generate forces and flows, forming a bath with active fluctuations. Two unanswered questions are whether those active agents can drive the assembly of passive components into unconventional states and which material properties they will exhibit. Here we show that passive, sticky beads immersed in a bath of swimming Escherichia coli bacteria aggregate into unconventional clusters and gels that are controlled by the activity of the bath. We observe a slow but persistent rotation of the aggregates that originates in the chirality of the E. coli flagella and directs aggregation into structures that are not accessible thermally. We elucidate the aggregation mechanism with a numerical model of spinning, sticky beads and reproduce quantitatively the experimental results. We show that internal activity controls the phase diagram and the structure of the aggregates. Overall, our results highlight the promising role of active baths in designing the structural and mechanical properties of materials with unconventional phases. acknowledgement: D.G. and J.P. thank E. Krasnopeeva, C. Guet, G. Guessous and T. Hwa for providing the E. coli strains. This material is based upon work supported by the US Department of Energy under award DE-SC0019769. I.P. acknowledges funding by the European Union’s Horizon 2020 research and innovation programme under Marie Skłodowska-Curie Grant Agreement No. 101034413. A.Š. acknowledges funding from the European Research Council under the European Union’s Horizon 2020 research and innovation programme (Grant No. 802960). M.C.U. acknowledges funding from the European Union’s Horizon 2020 research and innovation programme under Marie Skłodowska-Curie Grant Agreement No. 754411. article_processing_charge: Yes article_type: original author: - first_name: Daniel full_name: Grober, Daniel id: abdfc56f-34fb-11ee-bd33-fd766fce5a99 last_name: Grober - first_name: Ivan full_name: Palaia, Ivan id: 9c805cd2-4b75-11ec-a374-db6dd0ed57fa last_name: Palaia orcid: ' 0000-0002-8843-9485 ' - first_name: Mehmet C full_name: Ucar, Mehmet C id: 50B2A802-6007-11E9-A42B-EB23E6697425 last_name: Ucar orcid: 0000-0003-0506-4217 - first_name: Edouard B full_name: Hannezo, Edouard B id: 3A9DB764-F248-11E8-B48F-1D18A9856A87 last_name: Hannezo orcid: 0000-0001-6005-1561 - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Jérémie A full_name: Palacci, Jérémie A id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d last_name: Palacci orcid: 0000-0002-7253-9465 citation: ama: Grober D, Palaia I, Ucar MC, Hannezo EB, Šarić A, Palacci JA. Unconventional colloidal aggregation in chiral bacterial baths. Nature Physics. 2023;19:1680-1688. doi:10.1038/s41567-023-02136-x apa: Grober, D., Palaia, I., Ucar, M. C., Hannezo, E. B., Šarić, A., & Palacci, J. A. (2023). Unconventional colloidal aggregation in chiral bacterial baths. Nature Physics. Springer Nature. https://doi.org/10.1038/s41567-023-02136-x chicago: Grober, Daniel, Ivan Palaia, Mehmet C Ucar, Edouard B Hannezo, Anđela Šarić, and Jérémie A Palacci. “Unconventional Colloidal Aggregation in Chiral Bacterial Baths.” Nature Physics. Springer Nature, 2023. https://doi.org/10.1038/s41567-023-02136-x. ieee: D. Grober, I. Palaia, M. C. Ucar, E. B. Hannezo, A. Šarić, and J. A. Palacci, “Unconventional colloidal aggregation in chiral bacterial baths,” Nature Physics, vol. 19. Springer Nature, pp. 1680–1688, 2023. ista: Grober D, Palaia I, Ucar MC, Hannezo EB, Šarić A, Palacci JA. 2023. Unconventional colloidal aggregation in chiral bacterial baths. Nature Physics. 19, 1680–1688. mla: Grober, Daniel, et al. “Unconventional Colloidal Aggregation in Chiral Bacterial Baths.” Nature Physics, vol. 19, Springer Nature, 2023, pp. 1680–88, doi:10.1038/s41567-023-02136-x. short: D. Grober, I. Palaia, M.C. Ucar, E.B. Hannezo, A. Šarić, J.A. Palacci, Nature Physics 19 (2023) 1680–1688. corr_author: '1' date_created: 2023-08-06T22:01:11Z date_published: 2023-11-01T00:00:00Z date_updated: 2025-04-14T07:43:56Z day: '01' ddc: - '530' department: - _id: EdHa - _id: AnSa - _id: JePa doi: 10.1038/s41567-023-02136-x ec_funded: 1 external_id: isi: - '001037346400005' file: - access_level: open_access checksum: 7e282c2ebc0ac82125a04f6b4742d4c1 content_type: application/pdf creator: dernst date_created: 2024-01-30T12:26:08Z date_updated: 2024-01-30T12:26:08Z file_id: '14906' file_name: 2023_NaturePhysics_Grober.pdf file_size: 6365607 relation: main_file success: 1 file_date_updated: 2024-01-30T12:26:08Z has_accepted_license: '1' intvolume: ' 19' isi: 1 language: - iso: eng month: '11' oa: 1 oa_version: Published Version page: 1680-1688 project: - _id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c call_identifier: H2020 grant_number: '101034413' name: 'IST-BRIDGE: International postdoctoral program' - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' - _id: 260C2330-B435-11E9-9278-68D0E5697425 call_identifier: H2020 grant_number: '754411' name: ISTplus - Postdoctoral Fellowships publication: Nature Physics publication_identifier: eissn: - 1745-2481 issn: - 1745-2473 publication_status: published publisher: Springer Nature quality_controlled: '1' scopus_import: '1' status: public title: Unconventional colloidal aggregation in chiral bacterial baths tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 19 year: '2023' ... --- _id: '12708' 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. 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).' article_processing_charge: No article_type: original arxiv: 1 author: - first_name: Nuno A.M. full_name: Araújo, Nuno A.M. last_name: Araújo - first_name: Liesbeth M.C. full_name: Janssen, Liesbeth M.C. last_name: Janssen - first_name: Thomas full_name: Barois, Thomas last_name: Barois - first_name: Guido full_name: Boffetta, Guido last_name: Boffetta - first_name: Itai full_name: Cohen, Itai last_name: Cohen - first_name: Alessandro full_name: Corbetta, Alessandro last_name: Corbetta - first_name: Olivier full_name: Dauchot, Olivier last_name: Dauchot - first_name: Marjolein full_name: Dijkstra, Marjolein last_name: Dijkstra - first_name: William M. full_name: Durham, William M. last_name: Durham - first_name: Audrey full_name: Dussutour, Audrey last_name: Dussutour - first_name: Simon full_name: Garnier, Simon last_name: Garnier - first_name: Hanneke full_name: Gelderblom, Hanneke last_name: Gelderblom - first_name: Ramin full_name: Golestanian, Ramin last_name: Golestanian - first_name: Lucio full_name: Isa, Lucio last_name: Isa - first_name: Gijsje H. full_name: Koenderink, Gijsje H. last_name: Koenderink - first_name: Hartmut full_name: Löwen, Hartmut last_name: Löwen - first_name: Ralf full_name: Metzler, Ralf last_name: Metzler - first_name: Marco full_name: Polin, Marco last_name: Polin - first_name: C. Patrick full_name: Royall, C. Patrick last_name: Royall - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Anupam full_name: Sengupta, Anupam last_name: Sengupta - first_name: Cécile full_name: Sykes, Cécile last_name: Sykes - first_name: Vito full_name: Trianni, Vito last_name: Trianni - first_name: Idan full_name: Tuval, Idan last_name: Tuval - first_name: Nicolas full_name: Vogel, Nicolas last_name: Vogel - first_name: Julia M. full_name: Yeomans, Julia M. last_name: Yeomans - first_name: Iker full_name: Zuriguel, Iker last_name: Zuriguel - first_name: Alvaro full_name: Marin, Alvaro last_name: Marin - first_name: Giorgio full_name: Volpe, Giorgio last_name: Volpe citation: ama: Araújo NAM, Janssen LMC, Barois T, et al. Steering self-organisation through confinement. Soft Matter. 2023;19:1695-1704. doi:10.1039/d2sm01562e 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. Soft Matter. Royal Society of Chemistry. https://doi.org/10.1039/d2sm01562e 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.” Soft Matter. Royal Society of Chemistry, 2023. https://doi.org/10.1039/d2sm01562e. ieee: N. A. M. Araújo et al., “Steering self-organisation through confinement,” Soft Matter, vol. 19. Royal Society of Chemistry, pp. 1695–1704, 2023. 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. mla: Araújo, Nuno A. M., et al. “Steering Self-Organisation through Confinement.” Soft Matter, vol. 19, Royal Society of Chemistry, 2023, pp. 1695–704, doi:10.1039/d2sm01562e. 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. date_created: 2023-03-05T23:01:06Z date_published: 2023-02-06T00:00:00Z date_updated: 2025-04-23T08:48:51Z day: '06' ddc: - '540' department: - _id: AnSa doi: 10.1039/d2sm01562e ec_funded: 1 external_id: arxiv: - '2204.10059' isi: - '000940388100001' pmid: - '36779972' file: - access_level: open_access checksum: af95aa18b9b01e32fb8f13477c0e2687 content_type: application/pdf creator: cchlebak date_created: 2023-03-07T09:19:41Z date_updated: 2023-03-07T09:19:41Z file_id: '12711' file_name: 2023_SoftMatter_Araujo.pdf file_size: 3581939 relation: main_file success: 1 file_date_updated: 2023-03-07T09:19:41Z has_accepted_license: '1' intvolume: ' 19' isi: 1 language: - iso: eng month: '02' oa: 1 oa_version: Published Version page: 1695-1704 pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: Soft Matter publication_identifier: eissn: - 1744-6848 issn: - 1744-683X publication_status: published publisher: Royal Society of Chemistry quality_controlled: '1' scopus_import: '1' status: public title: Steering self-organisation through confinement tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 19 year: '2023' ... --- _id: '12756' abstract: - lang: eng 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. 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)." article_number: eade5224 article_processing_charge: No article_type: original author: - first_name: Fredrik full_name: Hurtig, Fredrik last_name: Hurtig - first_name: Thomas C.Q. full_name: Burgers, Thomas C.Q. last_name: Burgers - first_name: Alice full_name: Cezanne, Alice last_name: Cezanne - first_name: Xiuyun full_name: Jiang, Xiuyun last_name: Jiang - first_name: Frank N. full_name: Mol, Frank N. last_name: Mol - first_name: Jovan full_name: Traparić, Jovan last_name: Traparić - first_name: Andre Arashiro full_name: Pulschen, Andre Arashiro last_name: Pulschen - first_name: Tim full_name: Nierhaus, Tim last_name: Nierhaus - first_name: Gabriel full_name: Tarrason-Risa, Gabriel last_name: Tarrason-Risa - first_name: Lena full_name: Harker-Kirschneck, Lena last_name: Harker-Kirschneck - first_name: Jan full_name: Löwe, Jan last_name: Löwe - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Rifka full_name: Vlijm, Rifka last_name: Vlijm - first_name: Buzz full_name: Baum, Buzz last_name: Baum citation: 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. Science Advances. 2023;9(11). doi:10.1126/sciadv.ade5224 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. Science Advances. American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.ade5224 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.” Science Advances. American Association for the Advancement of Science, 2023. https://doi.org/10.1126/sciadv.ade5224. ieee: F. Hurtig et al., “The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division,” Science Advances, 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. mla: Hurtig, Fredrik, et al. “The Patterned Assembly and Stepwise Vps4-Mediated Disassembly of Composite ESCRT-III Polymers Drives Archaeal Cell Division.” Science Advances, vol. 9, no. 11, eade5224, American Association for the Advancement of Science, 2023, doi:10.1126/sciadv.ade5224. 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). corr_author: '1' date_created: 2023-03-26T22:01:06Z date_published: 2023-03-17T00:00:00Z date_updated: 2025-04-23T08:50:02Z day: '17' ddc: - '570' department: - _id: AnSa doi: 10.1126/sciadv.ade5224 ec_funded: 1 external_id: isi: - '000968083500010' pmid: - '36921039' file: - access_level: open_access checksum: 6d7dbe9ed86a116c8a002d62971202c5 content_type: application/pdf creator: dernst date_created: 2023-03-27T06:24:49Z date_updated: 2023-03-27T06:24:49Z file_id: '12768' file_name: 2023_ScienceAdvances_Hurtig.pdf file_size: 1826471 relation: main_file success: 1 file_date_updated: 2023-03-27T06:24:49Z has_accepted_license: '1' intvolume: ' 9' isi: 1 issue: '11' language: - iso: eng month: '03' oa: 1 oa_version: Published Version pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: Science Advances publication_identifier: eissn: - 2375-2548 publication_status: published publisher: American Association for the Advancement of Science quality_controlled: '1' scopus_import: '1' status: public title: The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 9 year: '2023' ... --- _id: '13094' abstract: - lang: eng text: 'Endocytosis is a key cellular process involved in the uptake of nutrients, pathogens, or the therapy of diseases. Most studies have focused on spherical objects, whereas biologically relevant shapes can be highly anisotropic. In this letter, we use an experimental model system based on Giant Unilamellar Vesicles (GUVs) and dumbbell-shaped colloidal particles to mimic and investigate the first stage of the passive endocytic process: engulfment of an anisotropic object by the membrane. Our model has specific ligand–receptor interactions realized by mobile receptors on the vesicles and immobile ligands on the particles. Through a series of experiments, theory, and molecular dynamics simulations, we quantify the wrapping process of anisotropic dumbbells by GUVs and identify distinct stages of the wrapping pathway. We find that the strong curvature variation in the neck of the dumbbell as well as membrane tension are crucial in determining both the speed of wrapping and the final states.' acknowledgement: We sincerely thank Casper van der Wel for providing open-source packages for tracking, as well as Yogesh Shelke for his assistance with PAA coverslip preparation and Rachel Doherty for her assistance with particle functionalization. We are grateful to Felix Frey for useful discussions on the theory of membrane wrapping. B.M. and A.Š. acknowledge funding by the European Union’s Horizon 2020 research and innovation programme (ERC Starting Grant No. 802960). article_processing_charge: No article_type: letter_note author: - first_name: Ali full_name: Azadbakht, Ali last_name: Azadbakht - first_name: Billie full_name: Meadowcroft, Billie id: a4725fd6-932b-11ed-81e2-c098c7f37ae1 last_name: Meadowcroft orcid: 0000-0003-3441-1337 - first_name: Thijs full_name: Varkevisser, Thijs last_name: Varkevisser - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Daniela J. full_name: Kraft, Daniela J. last_name: Kraft citation: ama: Azadbakht A, Meadowcroft B, Varkevisser T, Šarić A, Kraft DJ. Wrapping pathways of anisotropic dumbbell particles by Giant Unilamellar Vesicles. Nano Letters. 2023;23(10):4267–4273. doi:10.1021/acs.nanolett.3c00375 apa: Azadbakht, A., Meadowcroft, B., Varkevisser, T., Šarić, A., & Kraft, D. J. (2023). Wrapping pathways of anisotropic dumbbell particles by Giant Unilamellar Vesicles. Nano Letters. American Chemical Society. https://doi.org/10.1021/acs.nanolett.3c00375 chicago: Azadbakht, Ali, Billie Meadowcroft, Thijs Varkevisser, Anđela Šarić, and Daniela J. Kraft. “Wrapping Pathways of Anisotropic Dumbbell Particles by Giant Unilamellar Vesicles.” Nano Letters. American Chemical Society, 2023. https://doi.org/10.1021/acs.nanolett.3c00375. ieee: A. Azadbakht, B. Meadowcroft, T. Varkevisser, A. Šarić, and D. J. Kraft, “Wrapping pathways of anisotropic dumbbell particles by Giant Unilamellar Vesicles,” Nano Letters, vol. 23, no. 10. American Chemical Society, pp. 4267–4273, 2023. ista: Azadbakht A, Meadowcroft B, Varkevisser T, Šarić A, Kraft DJ. 2023. Wrapping pathways of anisotropic dumbbell particles by Giant Unilamellar Vesicles. Nano Letters. 23(10), 4267–4273. mla: Azadbakht, Ali, et al. “Wrapping Pathways of Anisotropic Dumbbell Particles by Giant Unilamellar Vesicles.” Nano Letters, vol. 23, no. 10, American Chemical Society, 2023, pp. 4267–4273, doi:10.1021/acs.nanolett.3c00375. short: A. Azadbakht, B. Meadowcroft, T. Varkevisser, A. Šarić, D.J. Kraft, Nano Letters 23 (2023) 4267–4273. date_created: 2023-05-28T22:01:03Z date_published: 2023-05-04T00:00:00Z date_updated: 2025-04-14T07:59:30Z day: '04' ddc: - '540' department: - _id: AnSa doi: 10.1021/acs.nanolett.3c00375 ec_funded: 1 external_id: isi: - '000985481400001' pmid: - '37141427' file: - access_level: open_access checksum: 9734d4c617bab3578ef62916b764547a content_type: application/pdf creator: dernst date_created: 2023-05-30T07:55:31Z date_updated: 2023-05-30T07:55:31Z file_id: '13100' file_name: 2023_NanoLetters_Azadbakht.pdf file_size: 3654910 relation: main_file success: 1 file_date_updated: 2023-05-30T07:55:31Z has_accepted_license: '1' intvolume: ' 23' isi: 1 issue: '10' language: - iso: eng month: '05' oa: 1 oa_version: Published Version page: 4267–4273 pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: Nano Letters publication_identifier: eissn: - 1530-6992 issn: - 1530-6984 publication_status: published publisher: American Chemical Society quality_controlled: '1' scopus_import: '1' status: public title: Wrapping pathways of anisotropic dumbbell particles by Giant Unilamellar Vesicles tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8 volume: 23 year: '2023' ... --- _id: '11841' abstract: - lang: eng text: Primary nucleation is the fundamental event that initiates the conversion of proteins from their normal physiological forms into pathological amyloid aggregates associated with the onset and development of disorders including systemic amyloidosis, as well as the neurodegenerative conditions Alzheimer’s and Parkinson’s diseases. It has become apparent that the presence of surfaces can dramatically modulate nucleation. However, the underlying physicochemical parameters governing this process have been challenging to elucidate, with interfaces in some cases having been found to accelerate aggregation, while in others they can inhibit the kinetics of this process. Here we show through kinetic analysis that for three different fibril-forming proteins, interfaces affect the aggregation reaction mainly through modulating the primary nucleation step. Moreover, we show through direct measurements of the Gibbs free energy of adsorption, combined with theory and coarse-grained computer simulations, that overall nucleation rates are suppressed at high and at low surface interaction strengths but significantly enhanced at intermediate strengths, and we verify these regimes experimentally. Taken together, these results provide a quantitative description of the fundamental process which triggers amyloid formation and shed light on the key factors that control this process. acknowledgement: "The research leading to these results has received funding from the European Research Council (ERC) under the European Union’s Seventh Framework Programme (FP7/2007-2013) through the ERC grant PhysProt\r\n(agreement 337969). We are grateful for financial support from the Biotechnology and Biological Sciences Research Council (BBSRC) (T.P.J.K.), the Newman\r\nFoundation (T.P.J.K.), the Wellcome Trust (T.P.J.K. and M.V.), Peterhouse College\r\nCambridge (T.C.T.M.), the ERC Starting Grant (StG) Non-Equilibrium Protein Assembly (NEPA) (A.S.), the Royal Society (A.S.), the Academy of Medical Sciences\r\n(A.S. and J.K.), and the Cambridge Centre for Misfolding Diseases (CMD)." article_number: e2109718119 article_processing_charge: No article_type: original author: - first_name: Zenon full_name: Toprakcioglu, Zenon last_name: Toprakcioglu - first_name: Ayaka full_name: Kamada, Ayaka last_name: Kamada - first_name: Thomas C.T. full_name: Michaels, Thomas C.T. last_name: Michaels - first_name: Mengqi full_name: Xie, Mengqi last_name: Xie - first_name: Johannes full_name: Krausser, Johannes last_name: Krausser - first_name: Jiapeng full_name: Wei, Jiapeng last_name: Wei - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Michele full_name: Vendruscolo, Michele last_name: Vendruscolo - first_name: Tuomas P.J. full_name: Knowles, Tuomas P.J. last_name: Knowles citation: ama: Toprakcioglu Z, Kamada A, Michaels TCT, et al. Adsorption free energy predicts amyloid protein nucleation rates. Proceedings of the National Academy of Sciences of the United States of America. 2022;119(31). doi:10.1073/pnas.2109718119 apa: Toprakcioglu, Z., Kamada, A., Michaels, T. C. T., Xie, M., Krausser, J., Wei, J., … Knowles, T. P. J. (2022). Adsorption free energy predicts amyloid protein nucleation rates. Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences. https://doi.org/10.1073/pnas.2109718119 chicago: Toprakcioglu, Zenon, Ayaka Kamada, Thomas C.T. Michaels, Mengqi Xie, Johannes Krausser, Jiapeng Wei, Anđela Šarić, Michele Vendruscolo, and Tuomas P.J. Knowles. “Adsorption Free Energy Predicts Amyloid Protein Nucleation Rates.” Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 2022. https://doi.org/10.1073/pnas.2109718119. ieee: Z. Toprakcioglu et al., “Adsorption free energy predicts amyloid protein nucleation rates,” Proceedings of the National Academy of Sciences of the United States of America, vol. 119, no. 31. National Academy of Sciences, 2022. ista: Toprakcioglu Z, Kamada A, Michaels TCT, Xie M, Krausser J, Wei J, Šarić A, Vendruscolo M, Knowles TPJ. 2022. Adsorption free energy predicts amyloid protein nucleation rates. Proceedings of the National Academy of Sciences of the United States of America. 119(31), e2109718119. mla: Toprakcioglu, Zenon, et al. “Adsorption Free Energy Predicts Amyloid Protein Nucleation Rates.” Proceedings of the National Academy of Sciences of the United States of America, vol. 119, no. 31, e2109718119, National Academy of Sciences, 2022, doi:10.1073/pnas.2109718119. short: Z. Toprakcioglu, A. Kamada, T.C.T. Michaels, M. Xie, J. Krausser, J. Wei, A. Šarić, M. Vendruscolo, T.P.J. Knowles, Proceedings of the National Academy of Sciences of the United States of America 119 (2022). date_created: 2022-08-14T22:01:45Z date_published: 2022-07-28T00:00:00Z date_updated: 2025-06-12T06:21:34Z day: '28' ddc: - '570' department: - _id: AnSa doi: 10.1073/pnas.2109718119 ec_funded: 1 external_id: isi: - '000903753500002' pmid: - '35901206' file: - access_level: open_access checksum: 0fe3878896cbeb6c44e29222ec2f336a content_type: application/pdf creator: dernst date_created: 2023-10-04T09:05:44Z date_updated: 2023-10-04T09:05:44Z file_id: '14386' file_name: 2022_PNAS_Toprakcioglu.pdf file_size: 2476021 relation: main_file success: 1 file_date_updated: 2023-10-04T09:05:44Z has_accepted_license: '1' intvolume: ' 119' isi: 1 issue: '31' language: - iso: eng month: '07' oa: 1 oa_version: Published Version pmid: 1 project: - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' publication: Proceedings of the National Academy of Sciences of the United States of America publication_identifier: eissn: - 1091-6490 issn: - 0027-8424 publication_status: published publisher: National Academy of Sciences quality_controlled: '1' scopus_import: '1' status: public title: Adsorption free energy predicts amyloid protein nucleation rates tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 119 year: '2022' ... --- _id: '12108' abstract: - lang: eng text: The sequential exchange of filament composition to increase filament curvature was proposed as a mechanism for how some biological polymers deform and cut membranes. The relationship between the filament composition and its mechanical effect is lacking. We develop a kinetic model for the assembly of composite filaments that includes protein–membrane adhesion, filament mechanics and membrane mechanics. We identify the physical conditions for such a membrane remodeling and show this mechanism of sequential polymer assembly lowers the energetic barrier for membrane deformation. acknowledgement: "We thank T. C. T. Michaels and J. Palacci for useful discussions. We thank Claudia Flandoli for the illustrations in Fig. 1(b) and Fig. 2. We acknowledge funding by the European Union’s Horizon 2020 Research and Innovation Programme under the Marie Skłodowska-Curie Grant\r\nAgreement No. 101034413 (I. P.), the Royal Society Grant No. UF160266 (A. Š.), the European Research Council under the European Union’s Horizon 2020 Research and Innovation Programme (Grant No. 802960; B. M., I. P., and A. Š.), and the Volkswagen Foundation\r\nLife Grant (B. B. and A. Š). " article_number: '268101' article_processing_charge: No article_type: original author: - first_name: Billie full_name: Meadowcroft, Billie id: a4725fd6-932b-11ed-81e2-c098c7f37ae1 last_name: Meadowcroft orcid: 0000-0003-3441-1337 - first_name: Ivan full_name: Palaia, Ivan id: 9c805cd2-4b75-11ec-a374-db6dd0ed57fa last_name: Palaia orcid: ' 0000-0002-8843-9485 ' - first_name: Anna Katharina full_name: Pfitzner, Anna Katharina last_name: Pfitzner - first_name: Aurélien full_name: Roux, Aurélien last_name: Roux - first_name: Buzz full_name: Baum, Buzz last_name: Baum - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 citation: ama: Meadowcroft B, Palaia I, Pfitzner AK, Roux A, Baum B, Šarić A. Mechanochemical rules for shape-shifting filaments that remodel membranes. Physical Review Letters. 2022;129(26). doi:10.1103/PhysRevLett.129.268101 apa: Meadowcroft, B., Palaia, I., Pfitzner, A. K., Roux, A., Baum, B., & Šarić, A. (2022). Mechanochemical rules for shape-shifting filaments that remodel membranes. Physical Review Letters. American Physical Society. https://doi.org/10.1103/PhysRevLett.129.268101 chicago: Meadowcroft, Billie, Ivan Palaia, Anna Katharina Pfitzner, Aurélien Roux, Buzz Baum, and Anđela Šarić. “Mechanochemical Rules for Shape-Shifting Filaments That Remodel Membranes.” Physical Review Letters. American Physical Society, 2022. https://doi.org/10.1103/PhysRevLett.129.268101. ieee: B. Meadowcroft, I. Palaia, A. K. Pfitzner, A. Roux, B. Baum, and A. Šarić, “Mechanochemical rules for shape-shifting filaments that remodel membranes,” Physical Review Letters, vol. 129, no. 26. American Physical Society, 2022. ista: Meadowcroft B, Palaia I, Pfitzner AK, Roux A, Baum B, Šarić A. 2022. Mechanochemical rules for shape-shifting filaments that remodel membranes. Physical Review Letters. 129(26), 268101. mla: Meadowcroft, Billie, et al. “Mechanochemical Rules for Shape-Shifting Filaments That Remodel Membranes.” Physical Review Letters, vol. 129, no. 26, 268101, American Physical Society, 2022, doi:10.1103/PhysRevLett.129.268101. short: B. Meadowcroft, I. Palaia, A.K. Pfitzner, A. Roux, B. Baum, A. Šarić, Physical Review Letters 129 (2022). corr_author: '1' date_created: 2023-01-08T23:00:53Z date_published: 2022-12-23T00:00:00Z date_updated: 2025-04-14T07:54:53Z day: '23' department: - _id: AnSa doi: 10.1103/PhysRevLett.129.268101 ec_funded: 1 external_id: isi: - '000906721500001' pmid: - '36608212' intvolume: ' 129' isi: 1 issue: '26' language: - iso: eng main_file_link: - open_access: '1' url: 'https://doi.org/10.1101/2022.05.10.490642 ' month: '12' oa: 1 oa_version: Preprint pmid: 1 project: - _id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c call_identifier: H2020 grant_number: '101034413' name: 'IST-BRIDGE: International postdoctoral program' - _id: eba2549b-77a9-11ec-83b8-a81e493eae4e call_identifier: H2020 grant_number: '802960' name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines' - _id: eba0f67c-77a9-11ec-83b8-cc8501b3e222 grant_number: '96752' name: 'The evolution of trafficking: from archaea to eukaryotes' publication: Physical Review Letters publication_identifier: eissn: - 1079-7114 issn: - 0031-9007 publication_status: published publisher: American Physical Society quality_controlled: '1' scopus_import: '1' status: public title: Mechanochemical rules for shape-shifting filaments that remodel membranes type: journal_article user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8 volume: 129 year: '2022' ...