--- _id: '10355' abstract: - lang: eng text: The molecular machinery of life is largely created via self-organisation of individual molecules into functional assemblies. Minimal coarse-grained models, in which a whole macromolecule is represented by a small number of particles, can be of great value in identifying the main driving forces behind self-organisation in cell biology. Such models can incorporate data from both molecular and continuum scales, and their results can be directly compared to experiments. Here we review the state of the art of models for studying the formation and biological function of macromolecular assemblies in living organisms. We outline the key ingredients of each model and their main findings. We illustrate the contribution of this class of simulations to identifying the physical mechanisms behind life and diseases, and discuss their future developments. acknowledgement: We acknowledge funding from EPSRC (A.E.H. and A.Š.), the Academy of Medical Sciences (J.K. and A.Š.), the Wellcome Trust (J.K. and A.Š.), and the Royal Society (A.Š.). We thank Shiladitya Banerjee and Nikola Ojkic for critically reading the manuscript, and Claudia Flandoli for helping us with figures and illustrations. article_processing_charge: No article_type: original author: - first_name: Anne E full_name: Hafner, Anne E last_name: Hafner - first_name: Johannes full_name: Krausser, Johannes last_name: Krausser - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 citation: ama: Hafner AE, Krausser J, Šarić A. Minimal coarse-grained models for molecular self-organisation in biology. Current Opinion in Structural Biology. 2019;58:43-52. doi:10.1016/j.sbi.2019.05.018 apa: Hafner, A. E., Krausser, J., & Šarić, A. (2019). Minimal coarse-grained models for molecular self-organisation in biology. Current Opinion in Structural Biology. Elsevier. https://doi.org/10.1016/j.sbi.2019.05.018 chicago: Hafner, Anne E, Johannes Krausser, and Anđela Šarić. “Minimal Coarse-Grained Models for Molecular Self-Organisation in Biology.” Current Opinion in Structural Biology. Elsevier, 2019. https://doi.org/10.1016/j.sbi.2019.05.018. ieee: A. E. Hafner, J. Krausser, and A. Šarić, “Minimal coarse-grained models for molecular self-organisation in biology,” Current Opinion in Structural Biology, vol. 58. Elsevier, pp. 43–52, 2019. ista: Hafner AE, Krausser J, Šarić A. 2019. Minimal coarse-grained models for molecular self-organisation in biology. Current Opinion in Structural Biology. 58, 43–52. mla: Hafner, Anne E., et al. “Minimal Coarse-Grained Models for Molecular Self-Organisation in Biology.” Current Opinion in Structural Biology, vol. 58, Elsevier, 2019, pp. 43–52, doi:10.1016/j.sbi.2019.05.018. short: A.E. Hafner, J. Krausser, A. Šarić, Current Opinion in Structural Biology 58 (2019) 43–52. date_created: 2021-11-26T11:33:21Z date_published: 2019-06-18T00:00:00Z date_updated: 2021-11-26T11:54:25Z day: '18' doi: 10.1016/j.sbi.2019.05.018 extern: '1' external_id: pmid: - '31226513' intvolume: ' 58' keyword: - molecular biology - structural biology language: - iso: eng main_file_link: - open_access: '1' url: https://arxiv.org/abs/1906.09349 month: '06' oa: 1 oa_version: Preprint page: 43-52 pmid: 1 publication: Current Opinion in Structural Biology publication_identifier: issn: - 0959-440X publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: Minimal coarse-grained models for molecular self-organisation in biology type: journal_article user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9 volume: 58 year: '2019' ... --- _id: '12190' abstract: - lang: eng text: Meiotic crossover frequency varies within genomes, which influences genetic diversity and adaptation. In turn, genetic variation within populations can act to modify crossover frequency in cis and trans. To identify genetic variation that controls meiotic crossover frequency, we screened Arabidopsis accessions using fluorescent recombination reporters. We mapped a genetic modifier of crossover frequency in Col × Bur populations of Arabidopsis to a premature stop codon within TBP-ASSOCIATED FACTOR 4b (TAF4b), which encodes a subunit of the RNA polymerase II general transcription factor TFIID. The Arabidopsis taf4b mutation is a rare variant found in the British Isles, originating in South-West Ireland. Using genetics, genomics, and immunocytology, we demonstrate a genome-wide decrease in taf4b crossovers, with strongest reduction in the sub-telomeric regions. Using RNA sequencing (RNA-seq) from purified meiocytes, we show that TAF4b expression is meiocyte enriched, whereas its paralog TAF4 is broadly expressed. Consistent with the role of TFIID in promoting gene expression, RNA-seq of wild-type and taf4b meiocytes identified widespread transcriptional changes, including in genes that regulate the meiotic cell cycle and recombination. Therefore, TAF4b duplication is associated with acquisition of meiocyte-specific expression and promotion of germline transcription, which act directly or indirectly to elevate crossovers. This identifies a novel mode of meiotic recombination control via a general transcription factor. acknowledgement: "We thank Gregory Copenhaver (University of North Carolina), Avraham Levy (The Weizmann Institute), and Scott Poethig (University of Pennsylvania) for FTLs; Piotr Ziolkowski for Col-420/Bur seed; Sureshkumar Balasubramanian\r\n(Monash University) for providing British and Irish Arabidopsis accessions; Mathilde Grelon (INRA, Versailles) for providing the MLH1 antibody; and the Gurdon Institute for access to microscopes. This work was supported by a BBSRC DTP studentship (E.J.L.), European Research Area Network for Coordinating Action in Plant Sciences/BBSRC ‘‘DeCOP’’ (BB/M004937/1; C.L.), a BBSRC David Phillips Fellowship (BB/L025043/1; H.G. and X.F.), the European Research Council (CoG ‘‘SynthHotspot,’’ A.J.T., C.L., and I.R.H.; StG ‘‘SexMeth,’’ X.F.), and a Sainsbury Charitable Foundation Studentship (A.R.B.)." article_processing_charge: No article_type: original author: - first_name: Emma J. full_name: Lawrence, Emma J. last_name: Lawrence - first_name: Hongbo full_name: Gao, Hongbo last_name: Gao - first_name: Andrew J. full_name: Tock, Andrew J. last_name: Tock - first_name: Christophe full_name: Lambing, Christophe last_name: Lambing - first_name: Alexander R. full_name: Blackwell, Alexander R. last_name: Blackwell - first_name: Xiaoqi full_name: Feng, Xiaoqi id: e0164712-22ee-11ed-b12a-d80fcdf35958 last_name: Feng orcid: 0000-0002-4008-1234 - first_name: Ian R. full_name: Henderson, Ian R. last_name: Henderson citation: ama: Lawrence EJ, Gao H, Tock AJ, et al. Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis. Current Biology. 2019;29(16):2676-2686.e3. doi:10.1016/j.cub.2019.06.084 apa: Lawrence, E. J., Gao, H., Tock, A. J., Lambing, C., Blackwell, A. R., Feng, X., & Henderson, I. R. (2019). Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis. Current Biology. Elsevier BV. https://doi.org/10.1016/j.cub.2019.06.084 chicago: Lawrence, Emma J., Hongbo Gao, Andrew J. Tock, Christophe Lambing, Alexander R. Blackwell, Xiaoqi Feng, and Ian R. Henderson. “Natural Variation in TBP-ASSOCIATED FACTOR 4b Controls Meiotic Crossover and Germline Transcription in Arabidopsis.” Current Biology. Elsevier BV, 2019. https://doi.org/10.1016/j.cub.2019.06.084. ieee: E. J. Lawrence et al., “Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis,” Current Biology, vol. 29, no. 16. Elsevier BV, p. 2676–2686.e3, 2019. ista: Lawrence EJ, Gao H, Tock AJ, Lambing C, Blackwell AR, Feng X, Henderson IR. 2019. Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis. Current Biology. 29(16), 2676–2686.e3. mla: Lawrence, Emma J., et al. “Natural Variation in TBP-ASSOCIATED FACTOR 4b Controls Meiotic Crossover and Germline Transcription in Arabidopsis.” Current Biology, vol. 29, no. 16, Elsevier BV, 2019, p. 2676–2686.e3, doi:10.1016/j.cub.2019.06.084. short: E.J. Lawrence, H. Gao, A.J. Tock, C. Lambing, A.R. Blackwell, X. Feng, I.R. Henderson, Current Biology 29 (2019) 2676–2686.e3. date_created: 2023-01-16T09:16:33Z date_published: 2019-08-19T00:00:00Z date_updated: 2023-05-08T10:54:54Z day: '19' department: - _id: XiFe doi: 10.1016/j.cub.2019.06.084 extern: '1' external_id: pmid: - '31378616' intvolume: ' 29' issue: '16' keyword: - General Agricultural and Biological Sciences - General Biochemistry - Genetics and Molecular Biology language: - iso: eng month: '08' oa_version: None page: 2676-2686.e3 pmid: 1 publication: Current Biology publication_identifier: issn: - 0960-9822 publication_status: published publisher: Elsevier BV quality_controlled: '1' scopus_import: '1' status: public title: Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 29 year: '2019' ... --- _id: '12192' abstract: - lang: eng text: Transposable elements (TEs), the movement of which can damage the genome, are epigenetically silenced in eukaryotes. Intriguingly, TEs are activated in the sperm companion cell – vegetative cell (VC) – of the flowering plant Arabidopsis thaliana. However, the extent and mechanism of this activation are unknown. Here we show that about 100 heterochromatic TEs are activated in VCs, mostly by DEMETER-catalyzed DNA demethylation. We further demonstrate that DEMETER access to some of these TEs is permitted by the natural depletion of linker histone H1 in VCs. Ectopically expressed H1 suppresses TEs in VCs by reducing DNA demethylation and via a methylation-independent mechanism. We demonstrate that H1 is required for heterochromatin condensation in plant cells and show that H1 overexpression creates heterochromatic foci in the VC progenitor cell. Taken together, our results demonstrate that the natural depletion of H1 during male gametogenesis facilitates DEMETER-directed DNA demethylation, heterochromatin relaxation, and TE activation. acknowledgement: We thank David Twell for the pDONR-P4-P1R-pLAT52 and pDONR-P2R-P3-mRFP vectors, the John Innes Centre Bioimaging Facility (Elaine Barclay and Grant Calder) for their assistance with microscopy, and the Norwich BioScience Institute Partnership Computing infrastructure for Science Group for High Performance Computing resources. This work was funded by a Biotechnology and Biological Sciences Research Council (BBSRC) David Phillips Fellowship (BB/L025043/1; SH, JZ and XF), a European Research Council Starting Grant ('SexMeth' 804981; XF) and a Grant to Exceptional Researchers by the Gatsby Charitable Foundation (SH and XF). article_number: '42530' article_processing_charge: No article_type: original author: - first_name: Shengbo full_name: He, Shengbo last_name: He - first_name: Martin full_name: Vickers, Martin last_name: Vickers - first_name: Jingyi full_name: Zhang, Jingyi last_name: Zhang - first_name: Xiaoqi full_name: Feng, Xiaoqi id: e0164712-22ee-11ed-b12a-d80fcdf35958 last_name: Feng orcid: 0000-0002-4008-1234 citation: ama: He S, Vickers M, Zhang J, Feng X. Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation. eLife. 2019;8. doi:10.7554/elife.42530 apa: He, S., Vickers, M., Zhang, J., & Feng, X. (2019). Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation. ELife. eLife Sciences Publications, Ltd. https://doi.org/10.7554/elife.42530 chicago: He, Shengbo, Martin Vickers, Jingyi Zhang, and Xiaoqi Feng. “Natural Depletion of Histone H1 in Sex Cells Causes DNA Demethylation, Heterochromatin Decondensation and Transposon Activation.” ELife. eLife Sciences Publications, Ltd, 2019. https://doi.org/10.7554/elife.42530. ieee: S. He, M. Vickers, J. Zhang, and X. Feng, “Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation,” eLife, vol. 8. eLife Sciences Publications, Ltd, 2019. ista: He S, Vickers M, Zhang J, Feng X. 2019. Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation. eLife. 8, 42530. mla: He, Shengbo, et al. “Natural Depletion of Histone H1 in Sex Cells Causes DNA Demethylation, Heterochromatin Decondensation and Transposon Activation.” ELife, vol. 8, 42530, eLife Sciences Publications, Ltd, 2019, doi:10.7554/elife.42530. short: S. He, M. Vickers, J. Zhang, X. Feng, ELife 8 (2019). date_created: 2023-01-16T09:17:21Z date_published: 2019-05-28T00:00:00Z date_updated: 2023-05-08T10:54:12Z day: '28' ddc: - '580' department: - _id: XiFe doi: 10.7554/elife.42530 extern: '1' external_id: unknown: - '31135340' file: - access_level: open_access checksum: ea6b89c20d59e5eb3646916fe5d568ad content_type: application/pdf creator: alisjak date_created: 2023-02-07T09:42:46Z date_updated: 2023-02-07T09:42:46Z file_id: '12525' file_name: 2019_elife_He.pdf file_size: 2493837 relation: main_file success: 1 file_date_updated: 2023-02-07T09:42:46Z has_accepted_license: '1' intvolume: ' 8' keyword: - General Immunology and Microbiology - General Biochemistry - Genetics and Molecular Biology - General Medicine - General Neuroscience language: - iso: eng main_file_link: - open_access: '1' url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6594752/ month: '05' oa: 1 oa_version: Published Version publication: eLife publication_identifier: issn: - 2050-084X publication_status: published publisher: eLife Sciences Publications, Ltd quality_controlled: '1' scopus_import: '1' status: public title: Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation 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: 8 year: '2019' ... --- _id: '10880' abstract: - lang: eng text: Acquisition of evolutionary novelties is a fundamental process for adapting to the external environment and invading new niches and results in the diversification of life, which we can see in the world today. How such novel phenotypic traits are acquired in the course of evolution and are built up in developing embryos has been a central question in biology. Whole-genome duplication (WGD) is a process of genome doubling that supplies raw genetic materials and increases genome complexity. Recently, it has been gradually revealed that WGD and subsequent fate changes of duplicated genes can facilitate phenotypic evolution. Here, we review the current understanding of the relationship between WGD and the acquisition of evolutionary novelties. We show some examples of this link and discuss how WGD and subsequent duplicated genes can facilitate phenotypic evolution as well as when such genomic doubling can be advantageous for adaptation. acknowledgement: This work was supported by JSPS overseas research fellowships (Y.M.) and SENSHIN Medical Research Foundation (K.K.T.). article_processing_charge: No article_type: original author: - first_name: Moriyama full_name: Yuuta, Moriyama id: 4968E7C8-F248-11E8-B48F-1D18A9856A87 last_name: Yuuta orcid: 0000-0002-2853-8051 - first_name: Kazuko full_name: Koshiba-Takeuchi, Kazuko last_name: Koshiba-Takeuchi citation: ama: Yuuta M, Koshiba-Takeuchi K. Significance of whole-genome duplications on the emergence of evolutionary novelties. Briefings in Functional Genomics. 2018;17(5):329-338. doi:10.1093/bfgp/ely007 apa: Yuuta, M., & Koshiba-Takeuchi, K. (2018). Significance of whole-genome duplications on the emergence of evolutionary novelties. Briefings in Functional Genomics. Oxford University Press. https://doi.org/10.1093/bfgp/ely007 chicago: Yuuta, Moriyama, and Kazuko Koshiba-Takeuchi. “Significance of Whole-Genome Duplications on the Emergence of Evolutionary Novelties.” Briefings in Functional Genomics. Oxford University Press, 2018. https://doi.org/10.1093/bfgp/ely007. ieee: M. Yuuta and K. Koshiba-Takeuchi, “Significance of whole-genome duplications on the emergence of evolutionary novelties,” Briefings in Functional Genomics, vol. 17, no. 5. Oxford University Press, pp. 329–338, 2018. ista: Yuuta M, Koshiba-Takeuchi K. 2018. Significance of whole-genome duplications on the emergence of evolutionary novelties. Briefings in Functional Genomics. 17(5), 329–338. mla: Yuuta, Moriyama, and Kazuko Koshiba-Takeuchi. “Significance of Whole-Genome Duplications on the Emergence of Evolutionary Novelties.” Briefings in Functional Genomics, vol. 17, no. 5, Oxford University Press, 2018, pp. 329–38, doi:10.1093/bfgp/ely007. short: M. Yuuta, K. Koshiba-Takeuchi, Briefings in Functional Genomics 17 (2018) 329–338. date_created: 2022-03-18T12:40:35Z date_published: 2018-09-01T00:00:00Z date_updated: 2023-09-19T15:11:22Z day: '01' department: - _id: CaHe doi: 10.1093/bfgp/ely007 external_id: isi: - '000456054400004' pmid: - '29579140' intvolume: ' 17' isi: 1 issue: '5' keyword: - Genetics - Molecular Biology - Biochemistry - General Medicine language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1093/bfgp/ely007 month: '09' oa: 1 oa_version: Published Version page: 329-338 pmid: 1 publication: Briefings in Functional Genomics publication_identifier: eissn: - 2041-2657 issn: - 2041-2649 publication_status: published publisher: Oxford University Press quality_controlled: '1' scopus_import: '1' status: public title: Significance of whole-genome duplications on the emergence of evolutionary novelties type: journal_article user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1 volume: 17 year: '2018' ... --- _id: '8436' abstract: - lang: eng text: The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local binding events. Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial “transfer-chaperone” system is able to guide α-helical and β-barrel membrane proteins in a “nascent chain-like” conformation through a ribosome-free compartment. article_processing_charge: No article_type: original author: - first_name: Katharina full_name: Weinhäupl, Katharina last_name: Weinhäupl - first_name: Caroline full_name: Lindau, Caroline last_name: Lindau - first_name: Audrey full_name: Hessel, Audrey last_name: Hessel - first_name: Yong full_name: Wang, Yong last_name: Wang - first_name: Conny full_name: Schütze, Conny last_name: Schütze - first_name: Tobias full_name: Jores, Tobias last_name: Jores - first_name: Laura full_name: Melchionda, Laura last_name: Melchionda - first_name: Birgit full_name: Schönfisch, Birgit last_name: Schönfisch - first_name: Hubert full_name: Kalbacher, Hubert last_name: Kalbacher - first_name: Beate full_name: Bersch, Beate last_name: Bersch - first_name: Doron full_name: Rapaport, Doron last_name: Rapaport - first_name: Martha full_name: Brennich, Martha last_name: Brennich - first_name: Kresten full_name: Lindorff-Larsen, Kresten last_name: Lindorff-Larsen - first_name: Nils full_name: Wiedemann, Nils last_name: Wiedemann - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. 2018;175(5):1365-1379.e25. doi:10.1016/j.cell.2018.10.039 apa: Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., … Schanda, P. (2018). Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. Elsevier. https://doi.org/10.1016/j.cell.2018.10.039 chicago: Weinhäupl, Katharina, Caroline Lindau, Audrey Hessel, Yong Wang, Conny Schütze, Tobias Jores, Laura Melchionda, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” Cell. Elsevier, 2018. https://doi.org/10.1016/j.cell.2018.10.039. ieee: K. Weinhäupl et al., “Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space,” Cell, vol. 175, no. 5. Elsevier, p. 1365–1379.e25, 2018. ista: Weinhäupl K, Lindau C, Hessel A, Wang Y, Schütze C, Jores T, Melchionda L, Schönfisch B, Kalbacher H, Bersch B, Rapaport D, Brennich M, Lindorff-Larsen K, Wiedemann N, Schanda P. 2018. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. 175(5), 1365–1379.e25. mla: Weinhäupl, Katharina, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” Cell, vol. 175, no. 5, Elsevier, 2018, p. 1365–1379.e25, doi:10.1016/j.cell.2018.10.039. short: K. Weinhäupl, C. Lindau, A. Hessel, Y. Wang, C. Schütze, T. Jores, L. Melchionda, B. Schönfisch, H. Kalbacher, B. Bersch, D. Rapaport, M. Brennich, K. Lindorff-Larsen, N. Wiedemann, P. Schanda, Cell 175 (2018) 1365–1379.e25. date_created: 2020-09-18T10:04:39Z date_published: 2018-11-15T00:00:00Z date_updated: 2021-01-12T08:19:15Z day: '15' doi: 10.1016/j.cell.2018.10.039 extern: '1' intvolume: ' 175' issue: '5' keyword: - General Biochemistry - Genetics and Molecular Biology language: - iso: eng month: '11' oa_version: None page: 1365-1379.e25 publication: Cell publication_identifier: issn: - 0092-8674 publication_status: published publisher: Elsevier quality_controlled: '1' status: public title: Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 175 year: '2018' ... --- _id: '8438' article_processing_charge: No article_type: letter_note author: - first_name: Vilius full_name: Kurauskas, Vilius last_name: Kurauskas - first_name: Audrey full_name: Hessel, Audrey last_name: Hessel - first_name: François full_name: Dehez, François last_name: Dehez - first_name: Christophe full_name: Chipot, Christophe last_name: Chipot - first_name: Beate full_name: Bersch, Beate last_name: Bersch - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. Dynamics and interactions of AAC3 in DPC are not functionally relevant. Nature Structural & Molecular Biology. 2018;25(9):745-747. doi:10.1038/s41594-018-0127-4 apa: Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., & Schanda, P. (2018). Dynamics and interactions of AAC3 in DPC are not functionally relevant. Nature Structural & Molecular Biology. Springer Nature. https://doi.org/10.1038/s41594-018-0127-4 chicago: Kurauskas, Vilius, Audrey Hessel, François Dehez, Christophe Chipot, Beate Bersch, and Paul Schanda. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally Relevant.” Nature Structural & Molecular Biology. Springer Nature, 2018. https://doi.org/10.1038/s41594-018-0127-4. ieee: V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, and P. Schanda, “Dynamics and interactions of AAC3 in DPC are not functionally relevant,” Nature Structural & Molecular Biology, vol. 25, no. 9. Springer Nature, pp. 745–747, 2018. ista: Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. 2018. Dynamics and interactions of AAC3 in DPC are not functionally relevant. Nature Structural & Molecular Biology. 25(9), 745–747. mla: Kurauskas, Vilius, et al. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally Relevant.” Nature Structural & Molecular Biology, vol. 25, no. 9, Springer Nature, 2018, pp. 745–47, doi:10.1038/s41594-018-0127-4. short: V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature Structural & Molecular Biology 25 (2018) 745–747. date_created: 2020-09-18T10:04:59Z date_published: 2018-09-03T00:00:00Z date_updated: 2021-01-12T08:19:16Z day: '03' doi: 10.1038/s41594-018-0127-4 extern: '1' intvolume: ' 25' issue: '9' keyword: - Molecular Biology - Structural Biology language: - iso: eng month: '09' oa_version: None page: 745-747 publication: Nature Structural & Molecular Biology publication_identifier: issn: - 1545-9993 - 1545-9985 publication_status: published publisher: Springer Nature quality_controlled: '1' status: public title: Dynamics and interactions of AAC3 in DPC are not functionally relevant type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 25 year: '2018' ... --- _id: '8439' abstract: - lang: eng text: Lipopolysaccharides (LPS) are complex glycolipids forming the outside layer of Gram-negative bacteria. Their hydrophobic and heterogeneous nature greatly hampers their structural study in an environment similar to the bacterial surface. We have studied LPS purified from E. coli and pathogenic P. aeruginosa with long O-antigen polysaccharides assembled in solution as vesicles or elongated micelles. Solid-state NMR with magic-angle spinning permitted the identification of NMR signals arising from regions with different flexibilities in the LPS, from the lipid components to the O-antigen polysaccharides. Atomic scale data on the LPS enabled the study of the interaction of gentamicin antibiotic bound to P. aeruginosa LPS, for which we could confirm that a specific oligosaccharide is involved in the antibiotic binding. The possibility to study LPS alone and bound to a ligand when it is assembled in membrane-like structures opens great prospects for the investigation of proteins and antibiotics that specifically target such an important molecule at the surface of Gram-negative bacteria. article_processing_charge: No article_type: original author: - first_name: Cedric full_name: Laguri, Cedric last_name: Laguri - first_name: Alba full_name: Silipo, Alba last_name: Silipo - first_name: Alessandra M. full_name: Martorana, Alessandra M. last_name: Martorana - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Roberta full_name: Marchetti, Roberta last_name: Marchetti - first_name: Alessandra full_name: Polissi, Alessandra last_name: Polissi - first_name: Antonio full_name: Molinaro, Antonio last_name: Molinaro - first_name: Jean-Pierre full_name: Simorre, Jean-Pierre last_name: Simorre citation: ama: Laguri C, Silipo A, Martorana AM, et al. Solid state NMR studies of intact lipopolysaccharide endotoxin. ACS Chemical Biology. 2018;13(8):2106-2113. doi:10.1021/acschembio.8b00271 apa: Laguri, C., Silipo, A., Martorana, A. M., Schanda, P., Marchetti, R., Polissi, A., … Simorre, J.-P. (2018). Solid state NMR studies of intact lipopolysaccharide endotoxin. ACS Chemical Biology. American Chemical Society. https://doi.org/10.1021/acschembio.8b00271 chicago: Laguri, Cedric, Alba Silipo, Alessandra M. Martorana, Paul Schanda, Roberta Marchetti, Alessandra Polissi, Antonio Molinaro, and Jean-Pierre Simorre. “Solid State NMR Studies of Intact Lipopolysaccharide Endotoxin.” ACS Chemical Biology. American Chemical Society, 2018. https://doi.org/10.1021/acschembio.8b00271. ieee: C. Laguri et al., “Solid state NMR studies of intact lipopolysaccharide endotoxin,” ACS Chemical Biology, vol. 13, no. 8. American Chemical Society, pp. 2106–2113, 2018. ista: Laguri C, Silipo A, Martorana AM, Schanda P, Marchetti R, Polissi A, Molinaro A, Simorre J-P. 2018. Solid state NMR studies of intact lipopolysaccharide endotoxin. ACS Chemical Biology. 13(8), 2106–2113. mla: Laguri, Cedric, et al. “Solid State NMR Studies of Intact Lipopolysaccharide Endotoxin.” ACS Chemical Biology, vol. 13, no. 8, American Chemical Society, 2018, pp. 2106–13, doi:10.1021/acschembio.8b00271. short: C. Laguri, A. Silipo, A.M. Martorana, P. Schanda, R. Marchetti, A. Polissi, A. Molinaro, J.-P. Simorre, ACS Chemical Biology 13 (2018) 2106–2113. date_created: 2020-09-18T10:05:09Z date_published: 2018-07-02T00:00:00Z date_updated: 2021-01-12T08:19:16Z day: '02' doi: 10.1021/acschembio.8b00271 extern: '1' intvolume: ' 13' issue: '8' keyword: - Molecular Medicine - Biochemistry - General Medicine language: - iso: eng month: '07' oa_version: None page: 2106-2113 publication: ACS Chemical Biology publication_identifier: issn: - 1554-8929 - 1554-8937 publication_status: published publisher: American Chemical Society quality_controlled: '1' status: public title: Solid state NMR studies of intact lipopolysaccharide endotoxin type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 13 year: '2018' ... --- _id: '8440' abstract: - lang: eng text: Mycobacterium tuberculosis can remain dormant in the host, an ability that explains the failure of many current tuberculosis treatments. Recently, the natural products cyclomarin, ecumicin, and lassomycin have been shown to efficiently kill Mycobacterium tuberculosis persisters. Their target is the N-terminal domain of the hexameric AAA+ ATPase ClpC1, which recognizes, unfolds, and translocates protein substrates, such as proteins containing phosphorylated arginine residues, to the ClpP1P2 protease for degradation. Surprisingly, these antibiotics do not inhibit ClpC1 ATPase activity, and how they cause cell death is still unclear. Here, using NMR and small-angle X-ray scattering, we demonstrate that arginine-phosphate binding to the ClpC1 N-terminal domain induces millisecond dynamics. We show that these dynamics are caused by conformational changes and do not result from unfolding or oligomerization of this domain. Cyclomarin binding to this domain specifically blocked these N-terminal dynamics. On the basis of these results, we propose a mechanism of action involving cyclomarin-induced restriction of ClpC1 dynamics, which modulates the chaperone enzymatic activity leading eventually to cell death. article_processing_charge: No article_type: original author: - first_name: Katharina full_name: Weinhäupl, Katharina last_name: Weinhäupl - first_name: Martha full_name: Brennich, Martha last_name: Brennich - first_name: Uli full_name: Kazmaier, Uli last_name: Kazmaier - first_name: Joel full_name: Lelievre, Joel last_name: Lelievre - first_name: Lluis full_name: Ballell, Lluis last_name: Ballell - first_name: Alfred full_name: Goldberg, Alfred last_name: Goldberg - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Hugo full_name: Fraga, Hugo last_name: Fraga citation: ama: Weinhäupl K, Brennich M, Kazmaier U, et al. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. 2018;293(22):8379-8393. doi:10.1074/jbc.ra118.002251 apa: Weinhäupl, K., Brennich, M., Kazmaier, U., Lelievre, J., Ballell, L., Goldberg, A., … Fraga, H. (2018). The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. American Society for Biochemistry & Molecular Biology. https://doi.org/10.1074/jbc.ra118.002251 chicago: Weinhäupl, Katharina, Martha Brennich, Uli Kazmaier, Joel Lelievre, Lluis Ballell, Alfred Goldberg, Paul Schanda, and Hugo Fraga. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” Journal of Biological Chemistry. American Society for Biochemistry & Molecular Biology, 2018. https://doi.org/10.1074/jbc.ra118.002251. ieee: K. Weinhäupl et al., “The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis,” Journal of Biological Chemistry, vol. 293, no. 22. American Society for Biochemistry & Molecular Biology, pp. 8379–8393, 2018. ista: Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda P, Fraga H. 2018. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. 293(22), 8379–8393. mla: Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” Journal of Biological Chemistry, vol. 293, no. 22, American Society for Biochemistry & Molecular Biology, 2018, pp. 8379–93, doi:10.1074/jbc.ra118.002251. short: K. Weinhäupl, M. Brennich, U. Kazmaier, J. Lelievre, L. Ballell, A. Goldberg, P. Schanda, H. Fraga, Journal of Biological Chemistry 293 (2018) 8379–8393. date_created: 2020-09-18T10:05:18Z date_published: 2018-06-01T00:00:00Z date_updated: 2021-01-12T08:19:17Z day: '01' doi: 10.1074/jbc.ra118.002251 extern: '1' intvolume: ' 293' issue: '22' keyword: - Cell Biology - Biochemistry - Molecular Biology language: - iso: eng month: '06' oa_version: None page: 8379-8393 publication: Journal of Biological Chemistry publication_identifier: issn: - 0021-9258 - 1083-351X publication_status: published publisher: American Society for Biochemistry & Molecular Biology quality_controlled: '1' status: public title: The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 293 year: '2018' ... --- _id: '13374' abstract: - lang: eng text: Confining molecules to volumes only slightly larger than the molecules themselves can profoundly alter their properties. Molecular switches—entities that can be toggled between two or more forms upon exposure to an external stimulus—often require conformational freedom to isomerize. Therefore, placing these switches in confined spaces can render them non-operational. To preserve the switchability of these species under confinement, we work with a water-soluble coordination cage that is flexible enough to adapt its shape to the conformation of the encapsulated guest. We show that owing to its flexibility, the cage is not only capable of accommodating—and solubilizing in water—several light-responsive spiropyran-based molecular switches, but, more importantly, it also provides an environment suitable for the efficient, reversible photoisomerization of the bound guests. Our findings pave the way towards studying various molecular switching processes in confined environments. article_number: '641' article_processing_charge: No article_type: original author: - first_name: Dipak full_name: Samanta, Dipak last_name: Samanta - first_name: Daria full_name: Galaktionova, Daria last_name: Galaktionova - first_name: Julius full_name: Gemen, Julius last_name: Gemen - first_name: Linda J. W. full_name: Shimon, Linda J. W. last_name: Shimon - first_name: Yael full_name: Diskin-Posner, Yael last_name: Diskin-Posner - first_name: Liat full_name: Avram, Liat last_name: Avram - first_name: Petr full_name: Král, Petr last_name: Král - first_name: Rafal full_name: Klajn, Rafal id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b last_name: Klajn citation: ama: Samanta D, Galaktionova D, Gemen J, et al. Reversible chromism of spiropyran in the cavity of a flexible coordination cage. Nature Communications. 2018;9. doi:10.1038/s41467-017-02715-6 apa: Samanta, D., Galaktionova, D., Gemen, J., Shimon, L. J. W., Diskin-Posner, Y., Avram, L., … Klajn, R. (2018). Reversible chromism of spiropyran in the cavity of a flexible coordination cage. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-017-02715-6 chicago: Samanta, Dipak, Daria Galaktionova, Julius Gemen, Linda J. W. Shimon, Yael Diskin-Posner, Liat Avram, Petr Král, and Rafal Klajn. “Reversible Chromism of Spiropyran in the Cavity of a Flexible Coordination Cage.” Nature Communications. Springer Nature, 2018. https://doi.org/10.1038/s41467-017-02715-6. ieee: D. Samanta et al., “Reversible chromism of spiropyran in the cavity of a flexible coordination cage,” Nature Communications, vol. 9. Springer Nature, 2018. ista: Samanta D, Galaktionova D, Gemen J, Shimon LJW, Diskin-Posner Y, Avram L, Král P, Klajn R. 2018. Reversible chromism of spiropyran in the cavity of a flexible coordination cage. Nature Communications. 9, 641. mla: Samanta, Dipak, et al. “Reversible Chromism of Spiropyran in the Cavity of a Flexible Coordination Cage.” Nature Communications, vol. 9, 641, Springer Nature, 2018, doi:10.1038/s41467-017-02715-6. short: D. Samanta, D. Galaktionova, J. Gemen, L.J.W. Shimon, Y. Diskin-Posner, L. Avram, P. Král, R. Klajn, Nature Communications 9 (2018). date_created: 2023-08-01T09:39:32Z date_published: 2018-02-13T00:00:00Z date_updated: 2023-08-07T10:54:05Z day: '13' doi: 10.1038/s41467-017-02715-6 extern: '1' external_id: pmid: - '29440687' intvolume: ' 9' keyword: - General Physics and Astronomy - General Biochemistry - Genetics and Molecular Biology - General Chemistry - Multidisciplinary language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1038/s41467-017-02715-6 month: '02' oa: 1 oa_version: Published Version pmid: 1 publication: Nature Communications publication_identifier: eissn: - 2041-1723 publication_status: published publisher: Springer Nature quality_controlled: '1' related_material: link: - relation: erratum url: https://doi.org/10.1038/s41467-018-03701-2 scopus_import: '1' status: public title: Reversible chromism of spiropyran in the cavity of a flexible coordination cage type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 9 year: '2018' ... --- _id: '14284' abstract: - lang: eng text: Pore-forming toxins (PFT) are virulence factors that transform from soluble to membrane-bound states. The Yersinia YaxAB system represents a family of binary α-PFTs with orthologues in human, insect, and plant pathogens, with unknown structures. YaxAB was shown to be cytotoxic and likely involved in pathogenesis, though the molecular basis for its two-component lytic mechanism remains elusive. Here, we present crystal structures of YaxA and YaxB, together with a cryo-electron microscopy map of the YaxAB complex. Our structures reveal a pore predominantly composed of decamers of YaxA–YaxB heterodimers. Both subunits bear membrane-active moieties, but only YaxA is capable of binding to membranes by itself. YaxB can subsequently be recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices. Pore formation can progress by further oligomerization of YaxA–YaxB dimers. Our results allow for a comparison between pore assemblies belonging to the wider ClyA-like family of α-PFTs, highlighting diverse pore architectures. article_number: '1806' article_processing_charge: No article_type: original author: - first_name: Bastian full_name: Bräuning, Bastian last_name: Bräuning - first_name: Eva full_name: Bertosin, Eva last_name: Bertosin - first_name: Florian M full_name: Praetorius, Florian M id: dfec9381-4341-11ee-8fd8-faa02bba7d62 last_name: Praetorius - first_name: Christian full_name: Ihling, Christian last_name: Ihling - first_name: Alexandra full_name: Schatt, Alexandra last_name: Schatt - first_name: Agnes full_name: Adler, Agnes last_name: Adler - first_name: Klaus full_name: Richter, Klaus last_name: Richter - first_name: Andrea full_name: Sinz, Andrea last_name: Sinz - first_name: Hendrik full_name: Dietz, Hendrik last_name: Dietz - first_name: Michael full_name: Groll, Michael last_name: Groll citation: ama: Bräuning B, Bertosin E, Praetorius FM, et al. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. Nature Communications. 2018;9. doi:10.1038/s41467-018-04139-2 apa: Bräuning, B., Bertosin, E., Praetorius, F. M., Ihling, C., Schatt, A., Adler, A., … Groll, M. (2018). Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-018-04139-2 chicago: Bräuning, Bastian, Eva Bertosin, Florian M Praetorius, Christian Ihling, Alexandra Schatt, Agnes Adler, Klaus Richter, Andrea Sinz, Hendrik Dietz, and Michael Groll. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” Nature Communications. Springer Nature, 2018. https://doi.org/10.1038/s41467-018-04139-2. ieee: B. Bräuning et al., “Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB,” Nature Communications, vol. 9. Springer Nature, 2018. ista: Bräuning B, Bertosin E, Praetorius FM, Ihling C, Schatt A, Adler A, Richter K, Sinz A, Dietz H, Groll M. 2018. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. Nature Communications. 9, 1806. mla: Bräuning, Bastian, et al. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” Nature Communications, vol. 9, 1806, Springer Nature, 2018, doi:10.1038/s41467-018-04139-2. short: B. Bräuning, E. Bertosin, F.M. Praetorius, C. Ihling, A. Schatt, A. Adler, K. Richter, A. Sinz, H. Dietz, M. Groll, Nature Communications 9 (2018). date_created: 2023-09-06T12:07:33Z date_published: 2018-05-04T00:00:00Z date_updated: 2023-11-07T11:46:12Z day: '04' doi: 10.1038/s41467-018-04139-2 extern: '1' external_id: pmid: - '29728606' intvolume: ' 9' keyword: - General Physics and Astronomy - General Biochemistry - Genetics and Molecular Biology - General Chemistry - Multidisciplinary language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1038/s41467-018-04139-2 month: '05' oa: 1 oa_version: Published Version pmid: 1 publication: Nature Communications publication_identifier: issn: - 2041-1723 publication_status: published publisher: Springer Nature quality_controlled: '1' scopus_import: '1' status: public title: Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 9 year: '2018' ... --- _id: '11065' abstract: - lang: eng text: Premature aging disorders provide an opportunity to study the mechanisms that drive aging. In Hutchinson-Gilford progeria syndrome (HGPS), a mutant form of the nuclear scaffold protein lamin A distorts nuclei and sequesters nuclear proteins. We sought to investigate protein homeostasis in this disease. Here, we report a widespread increase in protein turnover in HGPS-derived cells compared to normal cells. We determine that global protein synthesis is elevated as a consequence of activated nucleoli and enhanced ribosome biogenesis in HGPS-derived fibroblasts. Depleting normal lamin A or inducing mutant lamin A expression are each sufficient to drive nucleolar expansion. We further show that nucleolar size correlates with donor age in primary fibroblasts derived from healthy individuals and that ribosomal RNA production increases with age, indicating that nucleolar size and activity can serve as aging biomarkers. While limiting ribosome biogenesis extends lifespan in several systems, we show that increased ribosome biogenesis and activity are a hallmark of premature aging. article_number: '328' article_processing_charge: No article_type: original author: - first_name: Abigail full_name: Buchwalter, Abigail last_name: Buchwalter - first_name: Martin W full_name: HETZER, Martin W id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed last_name: HETZER orcid: 0000-0002-2111-992X citation: ama: Buchwalter A, Hetzer M. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 2017;8. doi:10.1038/s41467-017-00322-z apa: Buchwalter, A., & Hetzer, M. (2017). Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-017-00322-z chicago: Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” Nature Communications. Springer Nature, 2017. https://doi.org/10.1038/s41467-017-00322-z. ieee: A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” Nature Communications, vol. 8. Springer Nature, 2017. ista: Buchwalter A, Hetzer M. 2017. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 8, 328. mla: Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” Nature Communications, vol. 8, 328, Springer Nature, 2017, doi:10.1038/s41467-017-00322-z. short: A. Buchwalter, M. Hetzer, Nature Communications 8 (2017). date_created: 2022-04-07T07:45:50Z date_published: 2017-08-30T00:00:00Z date_updated: 2022-07-18T08:33:03Z day: '30' doi: 10.1038/s41467-017-00322-z extern: '1' external_id: pmid: - '28855503' intvolume: ' 8' keyword: - General Physics and Astronomy - General Biochemistry - Genetics and Molecular Biology - General Chemistry language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1038/s41467-017-00322-z month: '08' oa: 1 oa_version: Published Version pmid: 1 publication: Nature Communications publication_identifier: issn: - 2041-1723 publication_status: published publisher: Springer Nature quality_controlled: '1' scopus_import: '1' status: public title: Nucleolar expansion and elevated protein translation in premature aging type: journal_article user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd volume: 8 year: '2017' ... --- _id: '11067' abstract: - lang: eng text: Neural progenitor cells (NeuPCs) possess a unique nuclear architecture that changes during differentiation. Nucleoporins are linked with cell-type-specific gene regulation, coupling physical changes in nuclear structure to transcriptional output; but, whether and how they coordinate with key fate-determining transcription factors is unclear. Here we show that the nucleoporin Nup153 interacts with Sox2 in adult NeuPCs, where it is indispensable for their maintenance and controls neuronal differentiation. Genome-wide analyses show that Nup153 and Sox2 bind and co-regulate hundreds of genes. Binding of Nup153 to gene promoters or transcriptional end sites correlates with increased or decreased gene expression, respectively, and inhibiting Nup153 expression alters open chromatin configurations at its target genes, disrupts genomic localization of Sox2, and promotes differentiation in vitro and a gliogenic fate switch in vivo. Together, these findings reveal that nuclear structural proteins may exert bimodal transcriptional effects to control cell fate. article_processing_charge: No article_type: original author: - first_name: Tomohisa full_name: Toda, Tomohisa last_name: Toda - first_name: Jonathan Y. full_name: Hsu, Jonathan Y. last_name: Hsu - first_name: Sara B. full_name: Linker, Sara B. last_name: Linker - first_name: Lauren full_name: Hu, Lauren last_name: Hu - first_name: Simon T. full_name: Schafer, Simon T. last_name: Schafer - first_name: Jerome full_name: Mertens, Jerome last_name: Mertens - first_name: Filipe V. full_name: Jacinto, Filipe V. last_name: Jacinto - first_name: Martin W full_name: HETZER, Martin W id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed last_name: HETZER orcid: 0000-0002-2111-992X - first_name: Fred H. full_name: Gage, Fred H. last_name: Gage citation: ama: Toda T, Hsu JY, Linker SB, et al. Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells. Cell Stem Cell. 2017;21(5):618-634.e7. doi:10.1016/j.stem.2017.08.012 apa: Toda, T., Hsu, J. Y., Linker, S. B., Hu, L., Schafer, S. T., Mertens, J., … Gage, F. H. (2017). Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells. Cell Stem Cell. Elsevier. https://doi.org/10.1016/j.stem.2017.08.012 chicago: Toda, Tomohisa, Jonathan Y. Hsu, Sara B. Linker, Lauren Hu, Simon T. Schafer, Jerome Mertens, Filipe V. Jacinto, Martin Hetzer, and Fred H. Gage. “Nup153 Interacts with Sox2 to Enable Bimodal Gene Regulation and Maintenance of Neural Progenitor Cells.” Cell Stem Cell. Elsevier, 2017. https://doi.org/10.1016/j.stem.2017.08.012. ieee: T. Toda et al., “Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells,” Cell Stem Cell, vol. 21, no. 5. Elsevier, p. 618–634.e7, 2017. ista: Toda T, Hsu JY, Linker SB, Hu L, Schafer ST, Mertens J, Jacinto FV, Hetzer M, Gage FH. 2017. Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells. Cell Stem Cell. 21(5), 618–634.e7. mla: Toda, Tomohisa, et al. “Nup153 Interacts with Sox2 to Enable Bimodal Gene Regulation and Maintenance of Neural Progenitor Cells.” Cell Stem Cell, vol. 21, no. 5, Elsevier, 2017, p. 618–634.e7, doi:10.1016/j.stem.2017.08.012. short: T. Toda, J.Y. Hsu, S.B. Linker, L. Hu, S.T. Schafer, J. Mertens, F.V. Jacinto, M. Hetzer, F.H. Gage, Cell Stem Cell 21 (2017) 618–634.e7. date_created: 2022-04-07T07:46:12Z date_published: 2017-11-02T00:00:00Z date_updated: 2022-07-18T08:33:07Z day: '02' doi: 10.1016/j.stem.2017.08.012 extern: '1' external_id: pmid: - '28919367' intvolume: ' 21' issue: '5' keyword: - Cell Biology - Genetics - Molecular Medicine language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1016/j.stem.2017.08.012 month: '11' oa: 1 oa_version: Published Version page: 618-634.e7 pmid: 1 publication: Cell Stem Cell publication_identifier: issn: - 1934-5909 publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells type: journal_article user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd volume: 21 year: '2017' ... --- _id: '8446' abstract: - lang: eng text: Solid‐state NMR spectroscopy can provide insight into protein structure and dynamics at the atomic level without inherent protein size limitations. However, a major hurdle to studying large proteins by solid‐state NMR spectroscopy is related to spectral complexity and resonance overlap, which increase with molecular weight and severely hamper the assignment process. Here the use of two sets of experiments is shown to expand the tool kit of 1H‐detected assignment approaches, which correlate a given amide pair either to the two adjacent CO–CA pairs (4D hCOCANH/hCOCAcoNH), or to the amide 1H of the neighboring residue (3D HcocaNH/HcacoNH, which can be extended to 5D). The experiments are based on efficient coherence transfers between backbone atoms using INEPT transfers between carbons and cross‐polarization for heteronuclear transfers. The utility of these experiments is exemplified with application to assemblies of deuterated, fully amide‐protonated proteins from approximately 20 to 60 kDa monomer, at magic‐angle spinning (MAS) frequencies from approximately 40 to 55 kHz. These experiments will also be applicable to protonated proteins at higher MAS frequencies. The resonance assignment of a domain within the 50.4 kDa bacteriophage T5 tube protein pb6 is reported, and this is compared to NMR assignments of the isolated domain in solution. This comparison reveals contacts of this domain to the core of the polymeric tail tube assembly. article_processing_charge: No article_type: original author: - first_name: Hugo full_name: Fraga, Hugo last_name: Fraga - first_name: Charles‐Adrien full_name: Arnaud, Charles‐Adrien last_name: Arnaud - first_name: Diego F. full_name: Gauto, Diego F. last_name: Gauto - first_name: Maxime full_name: Audin, Maxime last_name: Audin - first_name: Vilius full_name: Kurauskas, Vilius last_name: Kurauskas - first_name: Pavel full_name: Macek, Pavel last_name: Macek - first_name: Carsten full_name: Krichel, Carsten last_name: Krichel - first_name: Jia‐Ying full_name: Guan, Jia‐Ying last_name: Guan - first_name: Jerome full_name: Boisbouvier, Jerome last_name: Boisbouvier - first_name: Remco full_name: Sprangers, Remco last_name: Sprangers - first_name: Cécile full_name: Breyton, Cécile last_name: Breyton - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Fraga H, Arnaud C, Gauto DF, et al. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. 2017;18(19):2697-2703. doi:10.1002/cphc.201700572 apa: Fraga, H., Arnaud, C., Gauto, D. F., Audin, M., Kurauskas, V., Macek, P., … Schanda, P. (2017). Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201700572 chicago: Fraga, Hugo, Charles‐Adrien Arnaud, Diego F. Gauto, Maxime Audin, Vilius Kurauskas, Pavel Macek, Carsten Krichel, et al. “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.” ChemPhysChem. Wiley, 2017. https://doi.org/10.1002/cphc.201700572. ieee: H. Fraga et al., “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins,” ChemPhysChem, vol. 18, no. 19. Wiley, pp. 2697–2703, 2017. ista: Fraga H, Arnaud C, Gauto DF, Audin M, Kurauskas V, Macek P, Krichel C, Guan J, Boisbouvier J, Sprangers R, Breyton C, Schanda P. 2017. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. 18(19), 2697–2703. mla: Fraga, Hugo, et al. “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.” ChemPhysChem, vol. 18, no. 19, Wiley, 2017, pp. 2697–703, doi:10.1002/cphc.201700572. short: H. Fraga, C. Arnaud, D.F. Gauto, M. Audin, V. Kurauskas, P. Macek, C. Krichel, J. Guan, J. Boisbouvier, R. Sprangers, C. Breyton, P. Schanda, ChemPhysChem 18 (2017) 2697–2703. date_created: 2020-09-18T10:06:09Z date_published: 2017-08-09T00:00:00Z date_updated: 2021-01-12T08:19:19Z day: '09' doi: 10.1002/cphc.201700572 extern: '1' intvolume: ' 18' issue: '19' keyword: - Physical and Theoretical Chemistry - Atomic and Molecular Physics - and Optics language: - iso: eng month: '08' oa_version: None page: 2697-2703 publication: ChemPhysChem publication_identifier: issn: - 1439-4235 - 1439-7641 publication_status: published publisher: Wiley quality_controlled: '1' status: public title: Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 18 year: '2017' ... --- _id: '14005' abstract: - lang: eng text: Strong-field photoelectron holography and laser-induced electron diffraction (LIED) are two powerful emerging methods for probing the ultrafast dynamics of molecules. However, both of them have remained restricted to static systems and to nuclear dynamics induced by strong-field ionization. Here we extend these promising methods to image purely electronic valence-shell dynamics in molecules using photoelectron holography. In the same experiment, we use LIED and photoelectron holography simultaneously, to observe coupled electronic-rotational dynamics taking place on similar timescales. These results offer perspectives for imaging ultrafast dynamics of molecules on femtosecond to attosecond timescales. article_number: '15651' article_processing_charge: No article_type: original author: - first_name: Samuel G. full_name: Walt, Samuel G. last_name: Walt - first_name: Niraghatam full_name: Bhargava Ram, Niraghatam last_name: Bhargava Ram - first_name: Marcos full_name: Atala, Marcos last_name: Atala - first_name: Nikolay I full_name: Shvetsov-Shilovski, Nikolay I last_name: Shvetsov-Shilovski - first_name: Aaron full_name: von Conta, Aaron last_name: von Conta - first_name: Denitsa Rangelova full_name: Baykusheva, Denitsa Rangelova id: 71b4d059-2a03-11ee-914d-dfa3beed6530 last_name: Baykusheva - first_name: Manfred full_name: Lein, Manfred last_name: Lein - first_name: Hans Jakob full_name: Wörner, Hans Jakob last_name: Wörner citation: ama: Walt SG, Bhargava Ram N, Atala M, et al. Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. Nature Communications. 2017;8. doi:10.1038/ncomms15651 apa: Walt, S. G., Bhargava Ram, N., Atala, M., Shvetsov-Shilovski, N. I., von Conta, A., Baykusheva, D. R., … Wörner, H. J. (2017). Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. Nature Communications. Springer Nature. https://doi.org/10.1038/ncomms15651 chicago: Walt, Samuel G., Niraghatam Bhargava Ram, Marcos Atala, Nikolay I Shvetsov-Shilovski, Aaron von Conta, Denitsa Rangelova Baykusheva, Manfred Lein, and Hans Jakob Wörner. “Dynamics of Valence-Shell Electrons and Nuclei Probed by Strong-Field Holography and Rescattering.” Nature Communications. Springer Nature, 2017. https://doi.org/10.1038/ncomms15651. ieee: S. G. Walt et al., “Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering,” Nature Communications, vol. 8. Springer Nature, 2017. ista: Walt SG, Bhargava Ram N, Atala M, Shvetsov-Shilovski NI, von Conta A, Baykusheva DR, Lein M, Wörner HJ. 2017. Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. Nature Communications. 8, 15651. mla: Walt, Samuel G., et al. “Dynamics of Valence-Shell Electrons and Nuclei Probed by Strong-Field Holography and Rescattering.” Nature Communications, vol. 8, 15651, Springer Nature, 2017, doi:10.1038/ncomms15651. short: S.G. Walt, N. Bhargava Ram, M. Atala, N.I. Shvetsov-Shilovski, A. von Conta, D.R. Baykusheva, M. Lein, H.J. Wörner, Nature Communications 8 (2017). date_created: 2023-08-10T06:36:09Z date_published: 2017-06-15T00:00:00Z date_updated: 2023-08-22T08:26:06Z day: '15' doi: 10.1038/ncomms15651 extern: '1' external_id: pmid: - '28643771' intvolume: ' 8' keyword: - General Physics and Astronomy - General Biochemistry - Genetics and Molecular Biology - General Chemistry - Multidisciplinary language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1038/ncomms15651 month: '06' oa: 1 oa_version: Published Version pmid: 1 publication: Nature Communications publication_identifier: eissn: - 2041-1723 publication_status: published publisher: Springer Nature quality_controlled: '1' scopus_import: '1' status: public title: Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 8 year: '2017' ... --- _id: '14007' abstract: - lang: eng text: 'In a recent article by Hockett et al (2016 J. Phys. B: At. Mol. Opt. Phys. 49 095602), time delays arising in the context of molecular single-photon ionization are investigated from a theoretical point of view. We argue that one of the central equations given in this article is incorrect and present a reformulation that is consistent with the established treatment of angle-dependent scattering delays (Eisenbud 1948 PhD Thesis Princeton University; Wigner 1955 Phys. Rev. 98 145–7; Smith 1960 Phys. Rev. 118 349–6; Nussenzveig 1972 Phys. Rev. D 6 1534–42).' article_number: '078002' article_processing_charge: No article_type: letter_note arxiv: 1 author: - first_name: Denitsa Rangelova full_name: Baykusheva, Denitsa Rangelova id: 71b4d059-2a03-11ee-914d-dfa3beed6530 last_name: Baykusheva - first_name: Hans Jakob full_name: Wörner, Hans Jakob last_name: Wörner citation: ama: 'Baykusheva DR, Wörner HJ. Comment on ‘Time delays in molecular photoionization.’ Journal of Physics B: Atomic, Molecular and Optical Physics. 2017;50(7). doi:10.1088/1361-6455/aa62b5' apa: 'Baykusheva, D. R., & Wörner, H. J. (2017). Comment on ‘Time delays in molecular photoionization.’ Journal of Physics B: Atomic, Molecular and Optical Physics. IOP Publishing. https://doi.org/10.1088/1361-6455/aa62b5' chicago: 'Baykusheva, Denitsa Rangelova, and Hans Jakob Wörner. “Comment on ‘Time Delays in Molecular Photoionization.’” Journal of Physics B: Atomic, Molecular and Optical Physics. IOP Publishing, 2017. https://doi.org/10.1088/1361-6455/aa62b5.' ieee: 'D. R. Baykusheva and H. J. Wörner, “Comment on ‘Time delays in molecular photoionization,’” Journal of Physics B: Atomic, Molecular and Optical Physics, vol. 50, no. 7. IOP Publishing, 2017.' ista: 'Baykusheva DR, Wörner HJ. 2017. Comment on ‘Time delays in molecular photoionization’. Journal of Physics B: Atomic, Molecular and Optical Physics. 50(7), 078002.' mla: 'Baykusheva, Denitsa Rangelova, and Hans Jakob Wörner. “Comment on ‘Time Delays in Molecular Photoionization.’” Journal of Physics B: Atomic, Molecular and Optical Physics, vol. 50, no. 7, 078002, IOP Publishing, 2017, doi:10.1088/1361-6455/aa62b5.' short: 'D.R. Baykusheva, H.J. Wörner, Journal of Physics B: Atomic, Molecular and Optical Physics 50 (2017).' date_created: 2023-08-10T06:36:29Z date_published: 2017-03-15T00:00:00Z date_updated: 2023-08-22T08:32:43Z day: '15' doi: 10.1088/1361-6455/aa62b5 extern: '1' external_id: arxiv: - '1611.09352' intvolume: ' 50' issue: '7' keyword: - Condensed Matter Physics - Atomic and Molecular Physics - and Optics language: - iso: eng main_file_link: - open_access: '1' url: https://arxiv.org/abs/1611.09352 month: '03' oa: 1 oa_version: Preprint publication: 'Journal of Physics B: Atomic, Molecular and Optical Physics' publication_identifier: eissn: - 1361-6455 issn: - 0953-4075 publication_status: published publisher: IOP Publishing quality_controlled: '1' scopus_import: '1' status: public title: Comment on ‘Time delays in molecular photoionization’ type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 50 year: '2017' ... --- _id: '10370' abstract: - lang: eng text: Eukaryotic cells are densely packed with macromolecular complexes and intertwining organelles, continually transported and reshaped. Intriguingly, organelles avoid clashing and entangling with each other in such limited space. Mitochondria form extensive networks constantly remodeled by fission and fusion. Here, we show that mitochondrial fission is triggered by mechanical forces. Mechano-stimulation of mitochondria – via encounter with motile intracellular pathogens, via external pressure applied by an atomic force microscope, or via cell migration across uneven microsurfaces – results in the recruitment of the mitochondrial fission machinery, and subsequent division. We propose that MFF, owing to affinity for narrow mitochondria, acts as a membrane-bound force sensor to recruit the fission machinery to mechanically strained sites. Thus, mitochondria adapt to the environment by sensing and responding to biomechanical cues. Our findings that mechanical triggers can be coupled to biochemical responses in membrane dynamics may explain how organelles orderly cohabit in the crowded cytoplasm. article_number: e30292 article_processing_charge: No article_type: original author: - first_name: Sebastian Carsten Johannes full_name: Helle, Sebastian Carsten Johannes last_name: Helle - first_name: Qian full_name: Feng, Qian last_name: Feng - first_name: Mathias J full_name: Aebersold, Mathias J last_name: Aebersold - first_name: Luca full_name: Hirt, Luca last_name: Hirt - first_name: Raphael R full_name: Grüter, Raphael R last_name: Grüter - first_name: Afshin full_name: Vahid, Afshin last_name: Vahid - first_name: Andrea full_name: Sirianni, Andrea last_name: Sirianni - first_name: Serge full_name: Mostowy, Serge last_name: Mostowy - first_name: Jess G full_name: Snedeker, Jess G last_name: Snedeker - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Timon full_name: Idema, Timon last_name: Idema - first_name: Tomaso full_name: Zambelli, Tomaso last_name: Zambelli - first_name: Benoît full_name: Kornmann, Benoît last_name: Kornmann citation: ama: Helle SCJ, Feng Q, Aebersold MJ, et al. Mechanical force induces mitochondrial fission. eLife. 2017;6. doi:10.7554/elife.30292 apa: Helle, S. C. J., Feng, Q., Aebersold, M. J., Hirt, L., Grüter, R. R., Vahid, A., … Kornmann, B. (2017). Mechanical force induces mitochondrial fission. ELife. eLife Sciences Publications. https://doi.org/10.7554/elife.30292 chicago: Helle, Sebastian Carsten Johannes, Qian Feng, Mathias J Aebersold, Luca Hirt, Raphael R Grüter, Afshin Vahid, Andrea Sirianni, et al. “Mechanical Force Induces Mitochondrial Fission.” ELife. eLife Sciences Publications, 2017. https://doi.org/10.7554/elife.30292. ieee: S. C. J. Helle et al., “Mechanical force induces mitochondrial fission,” eLife, vol. 6. eLife Sciences Publications, 2017. ista: Helle SCJ, Feng Q, Aebersold MJ, Hirt L, Grüter RR, Vahid A, Sirianni A, Mostowy S, Snedeker JG, Šarić A, Idema T, Zambelli T, Kornmann B. 2017. Mechanical force induces mitochondrial fission. eLife. 6, e30292. mla: Helle, Sebastian Carsten Johannes, et al. “Mechanical Force Induces Mitochondrial Fission.” ELife, vol. 6, e30292, eLife Sciences Publications, 2017, doi:10.7554/elife.30292. short: S.C.J. Helle, Q. Feng, M.J. Aebersold, L. Hirt, R.R. Grüter, A. Vahid, A. Sirianni, S. Mostowy, J.G. Snedeker, A. Šarić, T. Idema, T. Zambelli, B. Kornmann, ELife 6 (2017). date_created: 2021-11-29T08:51:38Z date_published: 2017-11-09T00:00:00Z date_updated: 2021-11-29T09:28:14Z day: '09' ddc: - '572' doi: 10.7554/elife.30292 extern: '1' external_id: pmid: - '29119945' file: - access_level: open_access checksum: c35f42dcfb007f6d6c761a27e24c26d3 content_type: application/pdf creator: cchlebak date_created: 2021-11-29T09:07:41Z date_updated: 2021-11-29T09:07:41Z file_id: '10372' file_name: 2017_eLife_Helle.pdf file_size: 6120157 relation: main_file success: 1 file_date_updated: 2021-11-29T09:07:41Z has_accepted_license: '1' intvolume: ' 6' keyword: - general immunology and microbiology - general biochemistry - genetics and molecular biology - general medicine - general neuroscience language: - iso: eng main_file_link: - open_access: '1' url: https://elifesciences.org/articles/30292 month: '11' oa: 1 oa_version: Published Version pmid: 1 publication: eLife publication_identifier: issn: - 2050-084X publication_status: published publisher: eLife Sciences Publications quality_controlled: '1' scopus_import: '1' status: public title: Mechanical force induces mitochondrial fission 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: 8b945eb4-e2f2-11eb-945a-df72226e66a9 volume: 6 year: '2017' ... --- _id: '11072' abstract: - lang: eng text: "Spatiotemporal activation of RhoA and actomyosin contraction underpins cellular adhesion and division. Loss of cell–cell adhesion and chromosomal instability are cardinal events that drive tumour progression. Here, we show that p120-catenin (p120) not only controls cell–cell adhesion, but also acts as a critical regulator of cytokinesis. We find that p120 regulates actomyosin contractility through concomitant binding to RhoA and the centralspindlin component MKLP1, independent of cadherin association. In anaphase, p120 is enriched at the cleavage furrow where it binds MKLP1 to spatially control RhoA GTPase cycling. Binding of p120 to MKLP1 during cytokinesis depends on the N-terminal coiled-coil domain of p120 isoform 1A. Importantly, clinical data show that loss of p120 expression is a common event in breast cancer that strongly correlates with multinucleation and adverse patient survival. In summary, our study identifies p120 loss as a driver event of chromosomal instability in cancer.\r\n" article_number: '13874' article_processing_charge: No article_type: original author: - first_name: Robert A.H. full_name: van de Ven, Robert A.H. last_name: van de Ven - first_name: Jolien S. full_name: de Groot, Jolien S. last_name: de Groot - first_name: Danielle full_name: Park, Danielle last_name: Park - first_name: Robert full_name: van Domselaar, Robert last_name: van Domselaar - first_name: Danielle full_name: de Jong, Danielle last_name: de Jong - first_name: Karoly full_name: Szuhai, Karoly last_name: Szuhai - first_name: Elsken full_name: van der Wall, Elsken last_name: van der Wall - first_name: Oscar M. full_name: Rueda, Oscar M. last_name: Rueda - first_name: H. Raza full_name: Ali, H. Raza last_name: Ali - first_name: Carlos full_name: Caldas, Carlos last_name: Caldas - first_name: Paul J. full_name: van Diest, Paul J. last_name: van Diest - first_name: Martin W full_name: HETZER, Martin W id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed last_name: HETZER orcid: 0000-0002-2111-992X - first_name: Erik full_name: Sahai, Erik last_name: Sahai - first_name: Patrick W.B. full_name: Derksen, Patrick W.B. last_name: Derksen citation: ama: van de Ven RAH, de Groot JS, Park D, et al. p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. Nature Communications. 2016;7. doi:10.1038/ncomms13874 apa: van de Ven, R. A. H., de Groot, J. S., Park, D., van Domselaar, R., de Jong, D., Szuhai, K., … Derksen, P. W. B. (2016). p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. Nature Communications. Springer Nature. https://doi.org/10.1038/ncomms13874 chicago: Ven, Robert A.H. van de, Jolien S. de Groot, Danielle Park, Robert van Domselaar, Danielle de Jong, Karoly Szuhai, Elsken van der Wall, et al. “P120-Catenin Prevents Multinucleation through Control of MKLP1-Dependent RhoA Activity during Cytokinesis.” Nature Communications. Springer Nature, 2016. https://doi.org/10.1038/ncomms13874. ieee: R. A. H. van de Ven et al., “p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis,” Nature Communications, vol. 7. Springer Nature, 2016. ista: van de Ven RAH, de Groot JS, Park D, van Domselaar R, de Jong D, Szuhai K, van der Wall E, Rueda OM, Ali HR, Caldas C, van Diest PJ, Hetzer M, Sahai E, Derksen PWB. 2016. p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. Nature Communications. 7, 13874. mla: van de Ven, Robert A. H., et al. “P120-Catenin Prevents Multinucleation through Control of MKLP1-Dependent RhoA Activity during Cytokinesis.” Nature Communications, vol. 7, 13874, Springer Nature, 2016, doi:10.1038/ncomms13874. short: R.A.H. van de Ven, J.S. de Groot, D. Park, R. van Domselaar, D. de Jong, K. Szuhai, E. van der Wall, O.M. Rueda, H.R. Ali, C. Caldas, P.J. van Diest, M. Hetzer, E. Sahai, P.W.B. Derksen, Nature Communications 7 (2016). date_created: 2022-04-07T07:48:34Z date_published: 2016-12-22T00:00:00Z date_updated: 2022-07-18T08:34:32Z day: '22' doi: 10.1038/ncomms13874 extern: '1' external_id: pmid: - '28004812' intvolume: ' 7' keyword: - General Physics and Astronomy - General Biochemistry - Genetics and Molecular Biology - General Chemistry language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1038/ncomms13874 month: '12' oa: 1 oa_version: Published Version pmid: 1 publication: Nature Communications publication_identifier: issn: - 2041-1723 publication_status: published publisher: Springer Nature quality_controlled: '1' related_material: link: - relation: erratum url: https://doi.org/10.1038/ncomms16030 scopus_import: '1' status: public title: p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis type: journal_article user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd volume: 7 year: '2016' ... --- _id: '13387' abstract: - lang: eng text: Come on in, the water's fine! Non-photoresponsive nanoparticles can be reversibly assembled using light by placing them in an aqueous solution of a photo­acid. Upon exposure to visible light, the photoacid reduces the pH of the solution, which induces attractive interactions between the nanoparticles. In the dark, the resulting nanoparticle aggregates spontaneously disassemble. The process can be repeated many times. article_processing_charge: No article_type: original author: - first_name: Dipak full_name: Samanta, Dipak last_name: Samanta - first_name: Rafal full_name: Klajn, Rafal id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b last_name: Klajn citation: ama: Samanta D, Klajn R. Aqueous light-controlled self-assembly of nanoparticles. Advanced Optical Materials. 2016;4(9):1373-1377. doi:10.1002/adom.201600364 apa: Samanta, D., & Klajn, R. (2016). Aqueous light-controlled self-assembly of nanoparticles. Advanced Optical Materials. Wiley. https://doi.org/10.1002/adom.201600364 chicago: Samanta, Dipak, and Rafal Klajn. “Aqueous Light-Controlled Self-Assembly of Nanoparticles.” Advanced Optical Materials. Wiley, 2016. https://doi.org/10.1002/adom.201600364. ieee: D. Samanta and R. Klajn, “Aqueous light-controlled self-assembly of nanoparticles,” Advanced Optical Materials, vol. 4, no. 9. Wiley, pp. 1373–1377, 2016. ista: Samanta D, Klajn R. 2016. Aqueous light-controlled self-assembly of nanoparticles. Advanced Optical Materials. 4(9), 1373–1377. mla: Samanta, Dipak, and Rafal Klajn. “Aqueous Light-Controlled Self-Assembly of Nanoparticles.” Advanced Optical Materials, vol. 4, no. 9, Wiley, 2016, pp. 1373–77, doi:10.1002/adom.201600364. short: D. Samanta, R. Klajn, Advanced Optical Materials 4 (2016) 1373–1377. date_created: 2023-08-01T09:42:49Z date_published: 2016-09-01T00:00:00Z date_updated: 2023-08-07T12:37:53Z day: '01' doi: 10.1002/adom.201600364 extern: '1' intvolume: ' 4' issue: '9' keyword: - Atomic and Molecular Physics - and Optics - Electronic - Optical and Magnetic Materials language: - iso: eng month: '09' oa_version: None page: 1373-1377 publication: Advanced Optical Materials publication_identifier: eissn: - 2195-1071 publication_status: published publisher: Wiley quality_controlled: '1' scopus_import: '1' status: public title: Aqueous light-controlled self-assembly of nanoparticles type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 4 year: '2016' ... --- _id: '13388' abstract: - lang: eng text: The Inside Cover picture illustrates the fluorescent properties of a gold nanocluster functionalized with several copies of a red-emitting merocyanine (image by Ella Marushchenko). The red fluorescence can be turned on and off reversibly by using an external stimulus. article_processing_charge: No author: - first_name: T. full_name: Udayabhaskararao, T. last_name: Udayabhaskararao - first_name: Pintu K. full_name: Kundu, Pintu K. last_name: Kundu - first_name: Johannes full_name: Ahrens, Johannes last_name: Ahrens - first_name: Rafal full_name: Klajn, Rafal id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b last_name: Klajn citation: ama: 'Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016). Vol 17. Wiley; 2016:1711-1711. doi:10.1002/cphc.201600480' apa: 'Udayabhaskararao, T., Kundu, P. K., Ahrens, J., & Klajn, R. (2016). Inside cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem 12/2016). ChemPhysChem (Vol. 17, pp. 1711–1711). Wiley. https://doi.org/10.1002/cphc.201600480' chicago: 'Udayabhaskararao, T., Pintu K. Kundu, Johannes Ahrens, and Rafal Klajn. Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016). ChemPhysChem. Vol. 17. Wiley, 2016. https://doi.org/10.1002/cphc.201600480.' ieee: 'T. Udayabhaskararao, P. K. Kundu, J. Ahrens, and R. Klajn, Inside cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem 12/2016), vol. 17, no. 12. Wiley, 2016, pp. 1711–1711.' ista: 'Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. 2016. Inside cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem 12/2016), Wiley,p.' mla: 'Udayabhaskararao, T., et al. “Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016).” ChemPhysChem, vol. 17, no. 12, Wiley, 2016, pp. 1711–1711, doi:10.1002/cphc.201600480.' short: 'T. Udayabhaskararao, P.K. Kundu, J. Ahrens, R. Klajn, Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016), Wiley, 2016.' date_created: 2023-08-01T09:43:07Z date_published: 2016-06-17T00:00:00Z date_updated: 2023-08-07T12:43:38Z day: '17' doi: 10.1002/cphc.201600480 extern: '1' intvolume: ' 17' issue: '12' keyword: - Physical and Theoretical Chemistry - Atomic and Molecular Physics - and Optics language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1002/cphc.201600480 month: '06' oa: 1 oa_version: Published Version page: 1711-1711 publication: ChemPhysChem publication_identifier: eissn: - 1439-7641 issn: - 1439-4235 publication_status: published publisher: Wiley quality_controlled: '1' status: public title: 'Inside cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem 12/2016)' type: other_academic_publication user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 17 year: '2016' ... --- _id: '13389' abstract: - lang: eng text: Au25 nanoclusters functionalized with a spiropyran molecular switch are synthesized via a ligand-exchange reaction at low temperature. The resulting nanoclusters are characterized by optical and NMR spectroscopies as well as by mass spectrometry. Spiropyran bound to nanoclusters isomerizes in a reversible fashion when exposed to UV and visible light, and its properties are similar to those of free spiropyran molecules in solution. The reversible photoisomerization entails the modulation of fluorescence as well as the light-controlled self-assembly of nanoclusters. article_processing_charge: No article_type: original author: - first_name: T. full_name: Udayabhaskararao, T. last_name: Udayabhaskararao - first_name: Pintu K. full_name: Kundu, Pintu K. last_name: Kundu - first_name: Johannes full_name: Ahrens, Johannes last_name: Ahrens - first_name: Rafal full_name: Klajn, Rafal id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b last_name: Klajn citation: ama: Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters. ChemPhysChem. 2016;17(12):1805-1809. doi:10.1002/cphc.201500897 apa: Udayabhaskararao, T., Kundu, P. K., Ahrens, J., & Klajn, R. (2016). Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201500897 chicago: Udayabhaskararao, T., Pintu K. Kundu, Johannes Ahrens, and Rafal Klajn. “Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters.” ChemPhysChem. Wiley, 2016. https://doi.org/10.1002/cphc.201500897. ieee: T. Udayabhaskararao, P. K. Kundu, J. Ahrens, and R. Klajn, “Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters,” ChemPhysChem, vol. 17, no. 12. Wiley, pp. 1805–1809, 2016. ista: Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. 2016. Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters. ChemPhysChem. 17(12), 1805–1809. mla: Udayabhaskararao, T., et al. “Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters.” ChemPhysChem, vol. 17, no. 12, Wiley, 2016, pp. 1805–09, doi:10.1002/cphc.201500897. short: T. Udayabhaskararao, P.K. Kundu, J. Ahrens, R. Klajn, ChemPhysChem 17 (2016) 1805–1809. date_created: 2023-08-01T09:43:18Z date_published: 2016-06-17T00:00:00Z date_updated: 2023-08-07T12:46:46Z day: '17' doi: 10.1002/cphc.201500897 extern: '1' external_id: pmid: - '26593975' intvolume: ' 17' issue: '12' keyword: - Physical and Theoretical Chemistry - Atomic and Molecular Physics - and Optics language: - iso: eng month: '06' oa_version: None page: 1805-1809 pmid: 1 publication: ChemPhysChem publication_identifier: eissn: - 1439-7641 issn: - 1439-4235 publication_status: published publisher: Wiley quality_controlled: '1' scopus_import: '1' status: public title: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 17 year: '2016' ...