[{"_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."}],"date_published":"2019-06-18T00:00:00Z","article_processing_charge":"No","volume":58,"oa":1,"main_file_link":[{"open_access":"1","url":"https://arxiv.org/abs/1906.09349"}],"publication_status":"published","oa_version":"Preprint","year":"2019","article_type":"original","publication_identifier":{"issn":["0959-440X"]},"date_updated":"2021-11-26T11:54:25Z","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","external_id":{"pmid":["31226513"]},"scopus_import":"1","date_created":"2021-11-26T11:33:21Z","extern":"1","month":"06","page":"43-52","status":"public","intvolume":"        58","quality_controlled":"1","publication":"Current Opinion in Structural Biology","publisher":"Elsevier","type":"journal_article","author":[{"first_name":"Anne E","full_name":"Hafner, Anne E","last_name":"Hafner"},{"full_name":"Krausser, Johannes","first_name":"Johannes","last_name":"Krausser"},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","orcid":"0000-0002-7854-2139","last_name":"Šarić","first_name":"Anđela","full_name":"Šarić, Anđela"}],"day":"18","title":"Minimal coarse-grained models for molecular self-organisation in biology","citation":{"mla":"Hafner, Anne E., et al. “Minimal Coarse-Grained Models for Molecular Self-Organisation in Biology.” <i>Current Opinion in Structural Biology</i>, vol. 58, Elsevier, 2019, pp. 43–52, doi:<a href=\"https://doi.org/10.1016/j.sbi.2019.05.018\">10.1016/j.sbi.2019.05.018</a>.","ieee":"A. E. Hafner, J. Krausser, and A. Šarić, “Minimal coarse-grained models for molecular self-organisation in biology,” <i>Current Opinion in Structural Biology</i>, 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.","chicago":"Hafner, Anne E, Johannes Krausser, and Anđela Šarić. “Minimal Coarse-Grained Models for Molecular Self-Organisation in Biology.” <i>Current Opinion in Structural Biology</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.sbi.2019.05.018\">https://doi.org/10.1016/j.sbi.2019.05.018</a>.","apa":"Hafner, A. E., Krausser, J., &#38; Šarić, A. (2019). Minimal coarse-grained models for molecular self-organisation in biology. <i>Current Opinion in Structural Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.sbi.2019.05.018\">https://doi.org/10.1016/j.sbi.2019.05.018</a>","ama":"Hafner AE, Krausser J, Šarić A. Minimal coarse-grained models for molecular self-organisation in biology. <i>Current Opinion in Structural Biology</i>. 2019;58:43-52. doi:<a href=\"https://doi.org/10.1016/j.sbi.2019.05.018\">10.1016/j.sbi.2019.05.018</a>","short":"A.E. Hafner, J. Krausser, A. Šarić, Current Opinion in Structural Biology 58 (2019) 43–52."},"doi":"10.1016/j.sbi.2019.05.018","language":[{"iso":"eng"}],"keyword":["molecular biology","structural biology"],"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.","pmid":1},{"scopus_import":"1","external_id":{"pmid":["31378616"]},"date_updated":"2023-05-08T10:54:54Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["0960-9822"]},"article_type":"original","year":"2019","oa_version":"None","publication_status":"published","volume":29,"article_processing_charge":"No","issue":"16","_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."}],"date_published":"2019-08-19T00:00:00Z","pmid":1,"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.).","keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"doi":"10.1016/j.cub.2019.06.084","citation":{"mla":"Lawrence, Emma J., et al. “Natural Variation in TBP-ASSOCIATED FACTOR 4b Controls Meiotic Crossover and Germline Transcription in Arabidopsis.” <i>Current Biology</i>, vol. 29, no. 16, Elsevier BV, 2019, p. 2676–2686.e3, doi:<a href=\"https://doi.org/10.1016/j.cub.2019.06.084\">10.1016/j.cub.2019.06.084</a>.","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.” <i>Current Biology</i>. Elsevier BV, 2019. <a href=\"https://doi.org/10.1016/j.cub.2019.06.084\">https://doi.org/10.1016/j.cub.2019.06.084</a>.","ieee":"E. J. Lawrence <i>et al.</i>, “Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis,” <i>Current Biology</i>, 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.","ama":"Lawrence EJ, Gao H, Tock AJ, et al. Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis. <i>Current Biology</i>. 2019;29(16):2676-2686.e3. doi:<a href=\"https://doi.org/10.1016/j.cub.2019.06.084\">10.1016/j.cub.2019.06.084</a>","apa":"Lawrence, E. J., Gao, H., Tock, A. J., Lambing, C., Blackwell, A. R., Feng, X., &#38; Henderson, I. R. (2019). Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis. <i>Current Biology</i>. Elsevier BV. <a href=\"https://doi.org/10.1016/j.cub.2019.06.084\">https://doi.org/10.1016/j.cub.2019.06.084</a>","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."},"title":"Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis","day":"19","author":[{"first_name":"Emma J.","full_name":"Lawrence, Emma J.","last_name":"Lawrence"},{"last_name":"Gao","first_name":"Hongbo","full_name":"Gao, Hongbo"},{"last_name":"Tock","first_name":"Andrew J.","full_name":"Tock, Andrew J."},{"full_name":"Lambing, Christophe","first_name":"Christophe","last_name":"Lambing"},{"full_name":"Blackwell, Alexander R.","first_name":"Alexander R.","last_name":"Blackwell"},{"orcid":"0000-0002-4008-1234","id":"e0164712-22ee-11ed-b12a-d80fcdf35958","full_name":"Feng, Xiaoqi","first_name":"Xiaoqi","last_name":"Feng"},{"first_name":"Ian R.","full_name":"Henderson, Ian R.","last_name":"Henderson"}],"type":"journal_article","publisher":"Elsevier BV","publication":"Current Biology","department":[{"_id":"XiFe"}],"quality_controlled":"1","status":"public","intvolume":"        29","page":"2676-2686.e3","month":"08","extern":"1","date_created":"2023-01-16T09:16:33Z"},{"author":[{"full_name":"He, Shengbo","first_name":"Shengbo","last_name":"He"},{"first_name":"Martin","full_name":"Vickers, Martin","last_name":"Vickers"},{"full_name":"Zhang, Jingyi","first_name":"Jingyi","last_name":"Zhang"},{"full_name":"Feng, Xiaoqi","first_name":"Xiaoqi","last_name":"Feng","id":"e0164712-22ee-11ed-b12a-d80fcdf35958","orcid":"0000-0002-4008-1234"}],"type":"journal_article","day":"28","title":"Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation","citation":{"mla":"He, Shengbo, et al. “Natural Depletion of Histone H1 in Sex Cells Causes DNA Demethylation, Heterochromatin Decondensation and Transposon Activation.” <i>ELife</i>, vol. 8, 42530, eLife Sciences Publications, Ltd, 2019, doi:<a href=\"https://doi.org/10.7554/elife.42530\">10.7554/elife.42530</a>.","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.","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,” <i>eLife</i>, vol. 8. eLife Sciences Publications, Ltd, 2019.","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.” <i>ELife</i>. eLife Sciences Publications, Ltd, 2019. <a href=\"https://doi.org/10.7554/elife.42530\">https://doi.org/10.7554/elife.42530</a>.","apa":"He, S., Vickers, M., Zhang, J., &#38; Feng, X. (2019). Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation. <i>ELife</i>. eLife Sciences Publications, Ltd. <a href=\"https://doi.org/10.7554/elife.42530\">https://doi.org/10.7554/elife.42530</a>","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. <i>eLife</i>. 2019;8. doi:<a href=\"https://doi.org/10.7554/elife.42530\">10.7554/elife.42530</a>","short":"S. He, M. Vickers, J. Zhang, X. Feng, ELife 8 (2019)."},"doi":"10.7554/elife.42530","ddc":["580"],"language":[{"iso":"eng"}],"keyword":["General Immunology and Microbiology","General Biochemistry","Genetics and Molecular Biology","General Medicine","General Neuroscience"],"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).","date_created":"2023-01-16T09:17:21Z","extern":"1","month":"05","intvolume":"         8","status":"public","quality_controlled":"1","department":[{"_id":"XiFe"}],"publication":"eLife","publisher":"eLife Sciences Publications, Ltd","year":"2019","has_accepted_license":"1","oa_version":"Published Version","article_type":"original","publication_identifier":{"issn":["2050-084X"]},"date_updated":"2023-05-08T10:54:12Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":"1","external_id":{"unknown":["31135340"]},"_id":"12192","date_published":"2019-05-28T00:00:00Z","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."}],"article_number":"42530","file":[{"file_name":"2019_elife_He.pdf","file_size":2493837,"creator":"alisjak","checksum":"ea6b89c20d59e5eb3646916fe5d568ad","date_updated":"2023-02-07T09:42:46Z","access_level":"open_access","content_type":"application/pdf","relation":"main_file","file_id":"12525","date_created":"2023-02-07T09:42:46Z","success":1}],"article_processing_charge":"No","volume":8,"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)"},"file_date_updated":"2023-02-07T09:42:46Z","main_file_link":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6594752/","open_access":"1"}],"oa":1,"publication_status":"published"},{"_id":"10880","date_published":"2018-09-01T00:00:00Z","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."}],"article_processing_charge":"No","issue":"5","volume":17,"publication_status":"published","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1093/bfgp/ely007"}],"oa":1,"article_type":"original","oa_version":"Published Version","year":"2018","external_id":{"pmid":["29579140"],"isi":["000456054400004"]},"scopus_import":"1","date_updated":"2023-09-19T15:11:22Z","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","publication_identifier":{"issn":["2041-2649"],"eissn":["2041-2657"]},"month":"09","date_created":"2022-03-18T12:40:35Z","page":"329-338","publication":"Briefings in Functional Genomics","department":[{"_id":"CaHe"}],"quality_controlled":"1","intvolume":"        17","status":"public","publisher":"Oxford University Press","isi":1,"day":"01","type":"journal_article","author":[{"last_name":"Yuuta","first_name":"Moriyama","full_name":"Yuuta, Moriyama","id":"4968E7C8-F248-11E8-B48F-1D18A9856A87","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. <i>Briefings in Functional Genomics</i>. 2018;17(5):329-338. doi:<a href=\"https://doi.org/10.1093/bfgp/ely007\">10.1093/bfgp/ely007</a>","apa":"Yuuta, M., &#38; Koshiba-Takeuchi, K. (2018). Significance of whole-genome duplications on the emergence of evolutionary novelties. <i>Briefings in Functional Genomics</i>. Oxford University Press. <a href=\"https://doi.org/10.1093/bfgp/ely007\">https://doi.org/10.1093/bfgp/ely007</a>","short":"M. Yuuta, K. Koshiba-Takeuchi, Briefings in Functional Genomics 17 (2018) 329–338.","mla":"Yuuta, Moriyama, and Kazuko Koshiba-Takeuchi. “Significance of Whole-Genome Duplications on the Emergence of Evolutionary Novelties.” <i>Briefings in Functional Genomics</i>, vol. 17, no. 5, Oxford University Press, 2018, pp. 329–38, doi:<a href=\"https://doi.org/10.1093/bfgp/ely007\">10.1093/bfgp/ely007</a>.","chicago":"Yuuta, Moriyama, and Kazuko Koshiba-Takeuchi. “Significance of Whole-Genome Duplications on the Emergence of Evolutionary Novelties.” <i>Briefings in Functional Genomics</i>. Oxford University Press, 2018. <a href=\"https://doi.org/10.1093/bfgp/ely007\">https://doi.org/10.1093/bfgp/ely007</a>.","ieee":"M. Yuuta and K. Koshiba-Takeuchi, “Significance of whole-genome duplications on the emergence of evolutionary novelties,” <i>Briefings in Functional Genomics</i>, 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."},"title":"Significance of whole-genome duplications on the emergence of evolutionary novelties","keyword":["Genetics","Molecular Biology","Biochemistry","General Medicine"],"language":[{"iso":"eng"}],"doi":"10.1093/bfgp/ely007","pmid":1,"acknowledgement":"This work was supported by JSPS overseas research fellowships (Y.M.) and SENSHIN Medical Research Foundation (K.K.T.)."},{"author":[{"last_name":"Weinhäupl","full_name":"Weinhäupl, Katharina","first_name":"Katharina"},{"last_name":"Lindau","first_name":"Caroline","full_name":"Lindau, Caroline"},{"last_name":"Hessel","first_name":"Audrey","full_name":"Hessel, Audrey"},{"first_name":"Yong","full_name":"Wang, Yong","last_name":"Wang"},{"last_name":"Schütze","first_name":"Conny","full_name":"Schütze, Conny"},{"full_name":"Jores, Tobias","first_name":"Tobias","last_name":"Jores"},{"last_name":"Melchionda","first_name":"Laura","full_name":"Melchionda, Laura"},{"first_name":"Birgit","full_name":"Schönfisch, Birgit","last_name":"Schönfisch"},{"first_name":"Hubert","full_name":"Kalbacher, Hubert","last_name":"Kalbacher"},{"last_name":"Bersch","first_name":"Beate","full_name":"Bersch, Beate"},{"last_name":"Rapaport","full_name":"Rapaport, Doron","first_name":"Doron"},{"full_name":"Brennich, Martha","first_name":"Martha","last_name":"Brennich"},{"last_name":"Lindorff-Larsen","full_name":"Lindorff-Larsen, Kresten","first_name":"Kresten"},{"last_name":"Wiedemann","first_name":"Nils","full_name":"Wiedemann, Nils"},{"last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"type":"journal_article","oa_version":"None","year":"2018","article_type":"original","day":"15","title":"Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space","citation":{"mla":"Weinhäupl, Katharina, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” <i>Cell</i>, vol. 175, no. 5, Elsevier, 2018, p. 1365–1379.e25, doi:<a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">10.1016/j.cell.2018.10.039</a>.","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.” <i>Cell</i>. Elsevier, 2018. <a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">https://doi.org/10.1016/j.cell.2018.10.039</a>.","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.","ieee":"K. Weinhäupl <i>et al.</i>, “Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space,” <i>Cell</i>, vol. 175, no. 5. Elsevier, p. 1365–1379.e25, 2018.","ama":"Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. <i>Cell</i>. 2018;175(5):1365-1379.e25. doi:<a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">10.1016/j.cell.2018.10.039</a>","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. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">https://doi.org/10.1016/j.cell.2018.10.039</a>","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."},"publication_identifier":{"issn":["0092-8674"]},"doi":"10.1016/j.cell.2018.10.039","keyword":["General Biochemistry","Genetics and Molecular Biology"],"date_updated":"2021-01-12T08:19:15Z","language":[{"iso":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"8436","date_created":"2020-09-18T10:04:39Z","date_published":"2018-11-15T00:00:00Z","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."}],"month":"11","extern":"1","article_processing_charge":"No","issue":"5","page":"1365-1379.e25","status":"public","intvolume":"       175","volume":175,"publication":"Cell","quality_controlled":"1","publisher":"Elsevier","publication_status":"published"},{"title":"Dynamics and interactions of AAC3 in DPC are not functionally relevant","citation":{"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,” <i>Nature Structural &#38; Molecular Biology</i>, 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 &#38; Molecular Biology. 25(9), 745–747.","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.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41594-018-0127-4\">https://doi.org/10.1038/s41594-018-0127-4</a>.","mla":"Kurauskas, Vilius, et al. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally Relevant.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 25, no. 9, Springer Nature, 2018, pp. 745–47, doi:<a href=\"https://doi.org/10.1038/s41594-018-0127-4\">10.1038/s41594-018-0127-4</a>.","short":"V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature Structural &#38; Molecular Biology 25 (2018) 745–747.","apa":"Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., &#38; Schanda, P. (2018). Dynamics and interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-018-0127-4\">https://doi.org/10.1038/s41594-018-0127-4</a>","ama":"Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. Dynamics and interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural &#38; Molecular Biology</i>. 2018;25(9):745-747. doi:<a href=\"https://doi.org/10.1038/s41594-018-0127-4\">10.1038/s41594-018-0127-4</a>"},"author":[{"last_name":"Kurauskas","first_name":"Vilius","full_name":"Kurauskas, Vilius"},{"last_name":"Hessel","first_name":"Audrey","full_name":"Hessel, Audrey"},{"first_name":"François","full_name":"Dehez, François","last_name":"Dehez"},{"last_name":"Chipot","first_name":"Christophe","full_name":"Chipot, Christophe"},{"first_name":"Beate","full_name":"Bersch, Beate","last_name":"Bersch"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda"}],"type":"journal_article","oa_version":"None","year":"2018","article_type":"letter_note","day":"03","publication_identifier":{"issn":["1545-9993","1545-9985"]},"doi":"10.1038/s41594-018-0127-4","keyword":["Molecular Biology","Structural Biology"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","language":[{"iso":"eng"}],"date_updated":"2021-01-12T08:19:16Z","article_processing_charge":"No","issue":"9","page":"745-747","date_created":"2020-09-18T10:04:59Z","_id":"8438","date_published":"2018-09-03T00:00:00Z","month":"09","extern":"1","publisher":"Springer Nature","publication_status":"published","status":"public","intvolume":"        25","volume":25,"publication":"Nature Structural & Molecular Biology","quality_controlled":"1"},{"publication_identifier":{"issn":["1554-8929","1554-8937"]},"doi":"10.1021/acschembio.8b00271","keyword":["Molecular Medicine","Biochemistry","General Medicine"],"language":[{"iso":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2021-01-12T08:19:16Z","title":"Solid state NMR studies of intact lipopolysaccharide endotoxin","citation":{"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.","ama":"Laguri C, Silipo A, Martorana AM, et al. Solid state NMR studies of intact lipopolysaccharide endotoxin. <i>ACS Chemical Biology</i>. 2018;13(8):2106-2113. doi:<a href=\"https://doi.org/10.1021/acschembio.8b00271\">10.1021/acschembio.8b00271</a>","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. <i>ACS Chemical Biology</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acschembio.8b00271\">https://doi.org/10.1021/acschembio.8b00271</a>","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.” <i>ACS Chemical Biology</i>. American Chemical Society, 2018. <a href=\"https://doi.org/10.1021/acschembio.8b00271\">https://doi.org/10.1021/acschembio.8b00271</a>.","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.","ieee":"C. Laguri <i>et al.</i>, “Solid state NMR studies of intact lipopolysaccharide endotoxin,” <i>ACS Chemical Biology</i>, vol. 13, no. 8. American Chemical Society, pp. 2106–2113, 2018.","mla":"Laguri, Cedric, et al. “Solid State NMR Studies of Intact Lipopolysaccharide Endotoxin.” <i>ACS Chemical Biology</i>, vol. 13, no. 8, American Chemical Society, 2018, pp. 2106–13, doi:<a href=\"https://doi.org/10.1021/acschembio.8b00271\">10.1021/acschembio.8b00271</a>."},"type":"journal_article","author":[{"last_name":"Laguri","full_name":"Laguri, Cedric","first_name":"Cedric"},{"full_name":"Silipo, Alba","first_name":"Alba","last_name":"Silipo"},{"last_name":"Martorana","first_name":"Alessandra M.","full_name":"Martorana, Alessandra M."},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul"},{"last_name":"Marchetti","first_name":"Roberta","full_name":"Marchetti, Roberta"},{"last_name":"Polissi","first_name":"Alessandra","full_name":"Polissi, Alessandra"},{"first_name":"Antonio","full_name":"Molinaro, Antonio","last_name":"Molinaro"},{"first_name":"Jean-Pierre","full_name":"Simorre, Jean-Pierre","last_name":"Simorre"}],"year":"2018","oa_version":"None","article_type":"original","day":"02","publication_status":"published","publisher":"American Chemical Society","intvolume":"        13","status":"public","volume":13,"publication":"ACS Chemical Biology","quality_controlled":"1","article_processing_charge":"No","issue":"8","page":"2106-2113","date_published":"2018-07-02T00:00:00Z","_id":"8439","abstract":[{"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.","lang":"eng"}],"date_created":"2020-09-18T10:05:09Z","month":"07","extern":"1"},{"keyword":["Cell Biology","Biochemistry","Molecular Biology"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2021-01-12T08:19:17Z","language":[{"iso":"eng"}],"publication_identifier":{"issn":["0021-9258","1083-351X"]},"doi":"10.1074/jbc.ra118.002251","citation":{"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.","ieee":"K. Weinhäupl <i>et al.</i>, “The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis,” <i>Journal of Biological Chemistry</i>, vol. 293, no. 22. American Society for Biochemistry &#38; Molecular Biology, pp. 8379–8393, 2018.","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.” <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology, 2018. <a href=\"https://doi.org/10.1074/jbc.ra118.002251\">https://doi.org/10.1074/jbc.ra118.002251</a>.","mla":"Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” <i>Journal of Biological Chemistry</i>, vol. 293, no. 22, American Society for Biochemistry &#38; Molecular Biology, 2018, pp. 8379–93, doi:<a href=\"https://doi.org/10.1074/jbc.ra118.002251\">10.1074/jbc.ra118.002251</a>.","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.","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. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology. <a href=\"https://doi.org/10.1074/jbc.ra118.002251\">https://doi.org/10.1074/jbc.ra118.002251</a>","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. <i>Journal of Biological Chemistry</i>. 2018;293(22):8379-8393. doi:<a href=\"https://doi.org/10.1074/jbc.ra118.002251\">10.1074/jbc.ra118.002251</a>"},"title":"The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis","article_type":"original","day":"01","author":[{"last_name":"Weinhäupl","full_name":"Weinhäupl, Katharina","first_name":"Katharina"},{"first_name":"Martha","full_name":"Brennich, Martha","last_name":"Brennich"},{"full_name":"Kazmaier, Uli","first_name":"Uli","last_name":"Kazmaier"},{"last_name":"Lelievre","full_name":"Lelievre, Joel","first_name":"Joel"},{"last_name":"Ballell","first_name":"Lluis","full_name":"Ballell, Lluis"},{"last_name":"Goldberg","full_name":"Goldberg, Alfred","first_name":"Alfred"},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda"},{"full_name":"Fraga, Hugo","first_name":"Hugo","last_name":"Fraga"}],"type":"journal_article","oa_version":"None","year":"2018","publisher":"American Society for Biochemistry & Molecular Biology","publication_status":"published","publication":"Journal of Biological Chemistry","quality_controlled":"1","intvolume":"       293","status":"public","volume":293,"page":"8379-8393","article_processing_charge":"No","issue":"22","month":"06","extern":"1","_id":"8440","abstract":[{"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.","lang":"eng"}],"date_created":"2020-09-18T10:05:18Z","date_published":"2018-06-01T00:00:00Z"},{"title":"Reversible chromism of spiropyran in the cavity of a flexible coordination cage","citation":{"ama":"Samanta D, Galaktionova D, Gemen J, et al. Reversible chromism of spiropyran in the cavity of a flexible coordination cage. <i>Nature Communications</i>. 2018;9. doi:<a href=\"https://doi.org/10.1038/s41467-017-02715-6\">10.1038/s41467-017-02715-6</a>","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. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-017-02715-6\">https://doi.org/10.1038/s41467-017-02715-6</a>","short":"D. Samanta, D. Galaktionova, J. Gemen, L.J.W. Shimon, Y. Diskin-Posner, L. Avram, P. Král, R. Klajn, Nature Communications 9 (2018).","mla":"Samanta, Dipak, et al. “Reversible Chromism of Spiropyran in the Cavity of a Flexible Coordination Cage.” <i>Nature Communications</i>, vol. 9, 641, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41467-017-02715-6\">10.1038/s41467-017-02715-6</a>.","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.” <i>Nature Communications</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41467-017-02715-6\">https://doi.org/10.1038/s41467-017-02715-6</a>.","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.","ieee":"D. Samanta <i>et al.</i>, “Reversible chromism of spiropyran in the cavity of a flexible coordination cage,” <i>Nature Communications</i>, vol. 9. Springer Nature, 2018."},"author":[{"first_name":"Dipak","full_name":"Samanta, Dipak","last_name":"Samanta"},{"last_name":"Galaktionova","first_name":"Daria","full_name":"Galaktionova, Daria"},{"full_name":"Gemen, Julius","first_name":"Julius","last_name":"Gemen"},{"full_name":"Shimon, Linda J. W.","first_name":"Linda J. W.","last_name":"Shimon"},{"last_name":"Diskin-Posner","full_name":"Diskin-Posner, Yael","first_name":"Yael"},{"last_name":"Avram","first_name":"Liat","full_name":"Avram, Liat"},{"last_name":"Král","full_name":"Král, Petr","first_name":"Petr"},{"last_name":"Klajn","full_name":"Klajn, Rafal","first_name":"Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"type":"journal_article","day":"13","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/s41467-018-03701-2"}]},"pmid":1,"doi":"10.1038/s41467-017-02715-6","language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"date_created":"2023-08-01T09:39:32Z","extern":"1","month":"02","publisher":"Springer Nature","status":"public","intvolume":"         9","quality_controlled":"1","publication":"Nature Communications","year":"2018","oa_version":"Published Version","article_type":"original","publication_identifier":{"eissn":["2041-1723"]},"date_updated":"2023-08-07T10:54:05Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"pmid":["29440687"]},"scopus_import":"1","article_processing_charge":"No","date_published":"2018-02-13T00:00:00Z","_id":"13374","abstract":[{"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.","lang":"eng"}],"article_number":"641","oa":1,"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-017-02715-6"}],"publication_status":"published","volume":9},{"date_created":"2023-09-06T12:07:33Z","extern":"1","month":"05","status":"public","intvolume":"         9","quality_controlled":"1","publication":"Nature Communications","publisher":"Springer Nature","type":"journal_article","author":[{"last_name":"Bräuning","full_name":"Bräuning, Bastian","first_name":"Bastian"},{"first_name":"Eva","full_name":"Bertosin, Eva","last_name":"Bertosin"},{"last_name":"Praetorius","first_name":"Florian M","full_name":"Praetorius, Florian M","id":"dfec9381-4341-11ee-8fd8-faa02bba7d62"},{"full_name":"Ihling, Christian","first_name":"Christian","last_name":"Ihling"},{"last_name":"Schatt","first_name":"Alexandra","full_name":"Schatt, Alexandra"},{"first_name":"Agnes","full_name":"Adler, Agnes","last_name":"Adler"},{"last_name":"Richter","full_name":"Richter, Klaus","first_name":"Klaus"},{"last_name":"Sinz","full_name":"Sinz, Andrea","first_name":"Andrea"},{"full_name":"Dietz, Hendrik","first_name":"Hendrik","last_name":"Dietz"},{"first_name":"Michael","full_name":"Groll, Michael","last_name":"Groll"}],"day":"04","title":"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB","citation":{"ama":"Bräuning B, Bertosin E, Praetorius FM, et al. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. <i>Nature Communications</i>. 2018;9. doi:<a href=\"https://doi.org/10.1038/s41467-018-04139-2\">10.1038/s41467-018-04139-2</a>","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. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>","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).","mla":"Bräuning, Bastian, et al. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” <i>Nature Communications</i>, vol. 9, 1806, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41467-018-04139-2\">10.1038/s41467-018-04139-2</a>.","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.” <i>Nature Communications</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>.","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.","ieee":"B. Bräuning <i>et al.</i>, “Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB,” <i>Nature Communications</i>, vol. 9. Springer Nature, 2018."},"doi":"10.1038/s41467-018-04139-2","language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"pmid":1,"date_published":"2018-05-04T00:00:00Z","_id":"14284","abstract":[{"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.","lang":"eng"}],"article_number":"1806","article_processing_charge":"No","volume":9,"oa":1,"main_file_link":[{"url":"https://doi.org/10.1038/s41467-018-04139-2","open_access":"1"}],"publication_status":"published","oa_version":"Published Version","year":"2018","article_type":"original","publication_identifier":{"issn":["2041-1723"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2023-11-07T11:46:12Z","external_id":{"pmid":["29728606"]},"scopus_import":"1"},{"article_type":"original","oa_version":"Published Version","year":"2017","external_id":{"pmid":["28855503"]},"scopus_import":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","date_updated":"2022-07-18T08:33:03Z","publication_identifier":{"issn":["2041-1723"]},"article_number":"328","date_published":"2017-08-30T00:00:00Z","_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_processing_charge":"No","volume":8,"publication_status":"published","main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-00322-z","open_access":"1"}],"oa":1,"day":"30","type":"journal_article","author":[{"last_name":"Buchwalter","full_name":"Buchwalter, Abigail","first_name":"Abigail"},{"first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"}],"citation":{"short":"A. Buchwalter, M. Hetzer, Nature Communications 8 (2017).","apa":"Buchwalter, A., &#38; Hetzer, M. (2017). Nucleolar expansion and elevated protein translation in premature aging. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-017-00322-z\">https://doi.org/10.1038/s41467-017-00322-z</a>","ama":"Buchwalter A, Hetzer M. Nucleolar expansion and elevated protein translation in premature aging. <i>Nature Communications</i>. 2017;8. doi:<a href=\"https://doi.org/10.1038/s41467-017-00322-z\">10.1038/s41467-017-00322-z</a>","ieee":"A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","ista":"Buchwalter A, Hetzer M. 2017. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 8, 328.","chicago":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” <i>Nature Communications</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1038/s41467-017-00322-z\">https://doi.org/10.1038/s41467-017-00322-z</a>.","mla":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” <i>Nature Communications</i>, vol. 8, 328, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/s41467-017-00322-z\">10.1038/s41467-017-00322-z</a>."},"title":"Nucleolar expansion and elevated protein translation in premature aging","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"language":[{"iso":"eng"}],"doi":"10.1038/s41467-017-00322-z","pmid":1,"month":"08","extern":"1","date_created":"2022-04-07T07:45:50Z","publication":"Nature Communications","quality_controlled":"1","intvolume":"         8","status":"public","publisher":"Springer Nature"},{"volume":21,"publication_status":"published","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.stem.2017.08.012"}],"oa":1,"_id":"11067","date_published":"2017-11-02T00:00:00Z","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","issue":"5","scopus_import":"1","external_id":{"pmid":["28919367"]},"date_updated":"2022-07-18T08:33:07Z","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication_identifier":{"issn":["1934-5909"]},"article_type":"original","year":"2017","oa_version":"Published Version","publication":"Cell Stem Cell","quality_controlled":"1","status":"public","intvolume":"        21","publisher":"Elsevier","month":"11","extern":"1","date_created":"2022-04-07T07:46:12Z","page":"618-634.e7","keyword":["Cell Biology","Genetics","Molecular Medicine"],"language":[{"iso":"eng"}],"doi":"10.1016/j.stem.2017.08.012","pmid":1,"day":"02","type":"journal_article","author":[{"full_name":"Toda, Tomohisa","first_name":"Tomohisa","last_name":"Toda"},{"full_name":"Hsu, Jonathan Y.","first_name":"Jonathan Y.","last_name":"Hsu"},{"last_name":"Linker","full_name":"Linker, Sara B.","first_name":"Sara B."},{"last_name":"Hu","full_name":"Hu, Lauren","first_name":"Lauren"},{"last_name":"Schafer","first_name":"Simon T.","full_name":"Schafer, Simon T."},{"full_name":"Mertens, Jerome","first_name":"Jerome","last_name":"Mertens"},{"full_name":"Jacinto, Filipe V.","first_name":"Filipe V.","last_name":"Jacinto"},{"full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"},{"full_name":"Gage, Fred H.","first_name":"Fred H.","last_name":"Gage"}],"citation":{"mla":"Toda, Tomohisa, et al. “Nup153 Interacts with Sox2 to Enable Bimodal Gene Regulation and Maintenance of Neural Progenitor Cells.” <i>Cell Stem Cell</i>, vol. 21, no. 5, Elsevier, 2017, p. 618–634.e7, doi:<a href=\"https://doi.org/10.1016/j.stem.2017.08.012\">10.1016/j.stem.2017.08.012</a>.","ieee":"T. Toda <i>et al.</i>, “Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells,” <i>Cell Stem Cell</i>, 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.","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.” <i>Cell Stem Cell</i>. Elsevier, 2017. <a href=\"https://doi.org/10.1016/j.stem.2017.08.012\">https://doi.org/10.1016/j.stem.2017.08.012</a>.","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. <i>Cell Stem Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.stem.2017.08.012\">https://doi.org/10.1016/j.stem.2017.08.012</a>","ama":"Toda T, Hsu JY, Linker SB, et al. Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells. <i>Cell Stem Cell</i>. 2017;21(5):618-634.e7. doi:<a href=\"https://doi.org/10.1016/j.stem.2017.08.012\">10.1016/j.stem.2017.08.012</a>","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."},"title":"Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells"},{"citation":{"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.” <i>ChemPhysChem</i>, vol. 18, no. 19, Wiley, 2017, pp. 2697–703, doi:<a href=\"https://doi.org/10.1002/cphc.201700572\">10.1002/cphc.201700572</a>.","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.” <i>ChemPhysChem</i>. Wiley, 2017. <a href=\"https://doi.org/10.1002/cphc.201700572\">https://doi.org/10.1002/cphc.201700572</a>.","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.","ieee":"H. Fraga <i>et al.</i>, “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins,” <i>ChemPhysChem</i>, vol. 18, no. 19. Wiley, pp. 2697–2703, 2017.","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. <i>ChemPhysChem</i>. 2017;18(19):2697-2703. doi:<a href=\"https://doi.org/10.1002/cphc.201700572\">10.1002/cphc.201700572</a>","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. <i>ChemPhysChem</i>. Wiley. <a href=\"https://doi.org/10.1002/cphc.201700572\">https://doi.org/10.1002/cphc.201700572</a>","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."},"title":"Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins","day":"09","article_type":"original","oa_version":"None","year":"2017","type":"journal_article","author":[{"last_name":"Fraga","first_name":"Hugo","full_name":"Fraga, Hugo"},{"first_name":"Charles‐Adrien","full_name":"Arnaud, Charles‐Adrien","last_name":"Arnaud"},{"last_name":"Gauto","first_name":"Diego F.","full_name":"Gauto, Diego F."},{"last_name":"Audin","first_name":"Maxime","full_name":"Audin, Maxime"},{"last_name":"Kurauskas","full_name":"Kurauskas, Vilius","first_name":"Vilius"},{"first_name":"Pavel","full_name":"Macek, Pavel","last_name":"Macek"},{"last_name":"Krichel","first_name":"Carsten","full_name":"Krichel, Carsten"},{"full_name":"Guan, Jia‐Ying","first_name":"Jia‐Ying","last_name":"Guan"},{"last_name":"Boisbouvier","full_name":"Boisbouvier, Jerome","first_name":"Jerome"},{"last_name":"Sprangers","full_name":"Sprangers, Remco","first_name":"Remco"},{"last_name":"Breyton","first_name":"Cécile","full_name":"Breyton, Cécile"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul"}],"date_updated":"2021-01-12T08:19:19Z","language":[{"iso":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"doi":"10.1002/cphc.201700572","publication_identifier":{"issn":["1439-4235","1439-7641"]},"page":"2697-2703","issue":"19","article_processing_charge":"No","extern":"1","month":"08","abstract":[{"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.","lang":"eng"}],"_id":"8446","date_created":"2020-09-18T10:06:09Z","date_published":"2017-08-09T00:00:00Z","publication_status":"published","publisher":"Wiley","quality_controlled":"1","publication":"ChemPhysChem","volume":18,"intvolume":"        18","status":"public"},{"publication":"Nature Communications","quality_controlled":"1","intvolume":"         8","status":"public","publisher":"Springer Nature","month":"06","extern":"1","date_created":"2023-08-10T06:36:09Z","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"language":[{"iso":"eng"}],"doi":"10.1038/ncomms15651","pmid":1,"day":"15","author":[{"last_name":"Walt","first_name":"Samuel G.","full_name":"Walt, Samuel G."},{"last_name":"Bhargava Ram","full_name":"Bhargava Ram, Niraghatam","first_name":"Niraghatam"},{"last_name":"Atala","first_name":"Marcos","full_name":"Atala, Marcos"},{"first_name":"Nikolay I","full_name":"Shvetsov-Shilovski, Nikolay I","last_name":"Shvetsov-Shilovski"},{"full_name":"von Conta, Aaron","first_name":"Aaron","last_name":"von Conta"},{"id":"71b4d059-2a03-11ee-914d-dfa3beed6530","first_name":"Denitsa Rangelova","full_name":"Baykusheva, Denitsa Rangelova","last_name":"Baykusheva"},{"last_name":"Lein","first_name":"Manfred","full_name":"Lein, Manfred"},{"full_name":"Wörner, Hans Jakob","first_name":"Hans Jakob","last_name":"Wörner"}],"type":"journal_article","citation":{"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. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms15651\">https://doi.org/10.1038/ncomms15651</a>","ama":"Walt SG, Bhargava Ram N, Atala M, et al. Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. <i>Nature Communications</i>. 2017;8. doi:<a href=\"https://doi.org/10.1038/ncomms15651\">10.1038/ncomms15651</a>","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).","mla":"Walt, Samuel G., et al. “Dynamics of Valence-Shell Electrons and Nuclei Probed by Strong-Field Holography and Rescattering.” <i>Nature Communications</i>, vol. 8, 15651, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/ncomms15651\">10.1038/ncomms15651</a>.","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.","ieee":"S. G. Walt <i>et al.</i>, “Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","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.” <i>Nature Communications</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1038/ncomms15651\">https://doi.org/10.1038/ncomms15651</a>."},"title":"Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering","volume":8,"publication_status":"published","main_file_link":[{"url":"https://doi.org/10.1038/ncomms15651","open_access":"1"}],"oa":1,"article_number":"15651","_id":"14005","date_published":"2017-06-15T00:00:00Z","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_processing_charge":"No","scopus_import":"1","external_id":{"pmid":["28643771"]},"date_updated":"2023-08-22T08:26:06Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"eissn":["2041-1723"]},"article_type":"original","year":"2017","oa_version":"Published Version"},{"publication_identifier":{"issn":["0953-4075"],"eissn":["1361-6455"]},"scopus_import":"1","external_id":{"arxiv":["1611.09352"]},"date_updated":"2023-08-22T08:32:43Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2017","oa_version":"Preprint","article_type":"letter_note","main_file_link":[{"url":"https://arxiv.org/abs/1611.09352","open_access":"1"}],"oa":1,"publication_status":"published","volume":50,"article_processing_charge":"No","issue":"7","arxiv":1,"_id":"14007","date_published":"2017-03-15T00:00:00Z","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","doi":"10.1088/1361-6455/aa62b5","keyword":["Condensed Matter Physics","Atomic and Molecular Physics","and Optics"],"language":[{"iso":"eng"}],"title":"Comment on ‘Time delays in molecular photoionization’","citation":{"ama":"Baykusheva DR, Wörner HJ. Comment on ‘Time delays in molecular photoionization.’ <i>Journal of Physics B: Atomic, Molecular and Optical Physics</i>. 2017;50(7). doi:<a href=\"https://doi.org/10.1088/1361-6455/aa62b5\">10.1088/1361-6455/aa62b5</a>","apa":"Baykusheva, D. R., &#38; Wörner, H. J. (2017). Comment on ‘Time delays in molecular photoionization.’ <i>Journal of Physics B: Atomic, Molecular and Optical Physics</i>. IOP Publishing. <a href=\"https://doi.org/10.1088/1361-6455/aa62b5\">https://doi.org/10.1088/1361-6455/aa62b5</a>","short":"D.R. Baykusheva, H.J. Wörner, Journal of Physics B: Atomic, Molecular and Optical Physics 50 (2017).","mla":"Baykusheva, Denitsa Rangelova, and Hans Jakob Wörner. “Comment on ‘Time Delays in Molecular Photoionization.’” <i>Journal of Physics B: Atomic, Molecular and Optical Physics</i>, vol. 50, no. 7, 078002, IOP Publishing, 2017, doi:<a href=\"https://doi.org/10.1088/1361-6455/aa62b5\">10.1088/1361-6455/aa62b5</a>.","chicago":"Baykusheva, Denitsa Rangelova, and Hans Jakob Wörner. “Comment on ‘Time Delays in Molecular Photoionization.’” <i>Journal of Physics B: Atomic, Molecular and Optical Physics</i>. IOP Publishing, 2017. <a href=\"https://doi.org/10.1088/1361-6455/aa62b5\">https://doi.org/10.1088/1361-6455/aa62b5</a>.","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.","ieee":"D. R. Baykusheva and H. J. Wörner, “Comment on ‘Time delays in molecular photoionization,’” <i>Journal of Physics B: Atomic, Molecular and Optical Physics</i>, vol. 50, no. 7. IOP Publishing, 2017."},"type":"journal_article","author":[{"full_name":"Baykusheva, Denitsa Rangelova","first_name":"Denitsa Rangelova","last_name":"Baykusheva","id":"71b4d059-2a03-11ee-914d-dfa3beed6530"},{"first_name":"Hans Jakob","full_name":"Wörner, Hans Jakob","last_name":"Wörner"}],"day":"15","publisher":"IOP Publishing","intvolume":"        50","status":"public","publication":"Journal of Physics B: Atomic, Molecular and Optical Physics","quality_controlled":"1","date_created":"2023-08-10T06:36:29Z","month":"03","extern":"1"},{"date_created":"2021-11-29T08:51:38Z","extern":"1","month":"11","intvolume":"         6","status":"public","quality_controlled":"1","publication":"eLife","publisher":"eLife Sciences Publications","type":"journal_article","author":[{"first_name":"Sebastian Carsten Johannes","full_name":"Helle, Sebastian Carsten Johannes","last_name":"Helle"},{"last_name":"Feng","full_name":"Feng, Qian","first_name":"Qian"},{"last_name":"Aebersold","first_name":"Mathias J","full_name":"Aebersold, Mathias J"},{"last_name":"Hirt","first_name":"Luca","full_name":"Hirt, Luca"},{"first_name":"Raphael R","full_name":"Grüter, Raphael R","last_name":"Grüter"},{"first_name":"Afshin","full_name":"Vahid, Afshin","last_name":"Vahid"},{"last_name":"Sirianni","full_name":"Sirianni, Andrea","first_name":"Andrea"},{"full_name":"Mostowy, Serge","first_name":"Serge","last_name":"Mostowy"},{"last_name":"Snedeker","first_name":"Jess G","full_name":"Snedeker, Jess G"},{"last_name":"Šarić","first_name":"Anđela","full_name":"Šarić, Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","orcid":"0000-0002-7854-2139"},{"last_name":"Idema","full_name":"Idema, Timon","first_name":"Timon"},{"first_name":"Tomaso","full_name":"Zambelli, Tomaso","last_name":"Zambelli"},{"first_name":"Benoît","full_name":"Kornmann, Benoît","last_name":"Kornmann"}],"day":"09","title":"Mechanical force induces mitochondrial fission","citation":{"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).","ama":"Helle SCJ, Feng Q, Aebersold MJ, et al. Mechanical force induces mitochondrial fission. <i>eLife</i>. 2017;6. doi:<a href=\"https://doi.org/10.7554/elife.30292\">10.7554/elife.30292</a>","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. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/elife.30292\">https://doi.org/10.7554/elife.30292</a>","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.” <i>ELife</i>. eLife Sciences Publications, 2017. <a href=\"https://doi.org/10.7554/elife.30292\">https://doi.org/10.7554/elife.30292</a>.","ieee":"S. C. J. Helle <i>et al.</i>, “Mechanical force induces mitochondrial fission,” <i>eLife</i>, 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.” <i>ELife</i>, vol. 6, e30292, eLife Sciences Publications, 2017, doi:<a href=\"https://doi.org/10.7554/elife.30292\">10.7554/elife.30292</a>."},"doi":"10.7554/elife.30292","ddc":["572"],"language":[{"iso":"eng"}],"keyword":["general immunology and microbiology","general biochemistry","genetics and molecular biology","general medicine","general neuroscience"],"pmid":1,"_id":"10370","date_published":"2017-11-09T00:00:00Z","abstract":[{"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.","lang":"eng"}],"article_number":"e30292","file":[{"access_level":"open_access","date_updated":"2021-11-29T09:07:41Z","checksum":"c35f42dcfb007f6d6c761a27e24c26d3","creator":"cchlebak","file_size":6120157,"file_name":"2017_eLife_Helle.pdf","success":1,"date_created":"2021-11-29T09:07:41Z","relation":"main_file","file_id":"10372","content_type":"application/pdf"}],"article_processing_charge":"No","volume":6,"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)"},"file_date_updated":"2021-11-29T09:07:41Z","oa":1,"main_file_link":[{"open_access":"1","url":"https://elifesciences.org/articles/30292"}],"publication_status":"published","has_accepted_license":"1","oa_version":"Published Version","year":"2017","article_type":"original","publication_identifier":{"issn":["2050-084X"]},"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","date_updated":"2021-11-29T09:28:14Z","scopus_import":"1","external_id":{"pmid":["29119945"]}},{"_id":"11072","abstract":[{"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","lang":"eng"}],"date_published":"2016-12-22T00:00:00Z","article_number":"13874","article_processing_charge":"No","volume":7,"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms13874"}],"oa":1,"publication_status":"published","year":"2016","oa_version":"Published Version","article_type":"original","publication_identifier":{"issn":["2041-1723"]},"date_updated":"2022-07-18T08:34:32Z","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","scopus_import":"1","external_id":{"pmid":["28004812"]},"date_created":"2022-04-07T07:48:34Z","extern":"1","month":"12","intvolume":"         7","status":"public","quality_controlled":"1","publication":"Nature Communications","publisher":"Springer Nature","type":"journal_article","author":[{"last_name":"van de Ven","first_name":"Robert A.H.","full_name":"van de Ven, Robert A.H."},{"first_name":"Jolien S.","full_name":"de Groot, Jolien S.","last_name":"de Groot"},{"last_name":"Park","first_name":"Danielle","full_name":"Park, Danielle"},{"first_name":"Robert","full_name":"van Domselaar, Robert","last_name":"van Domselaar"},{"last_name":"de Jong","full_name":"de Jong, Danielle","first_name":"Danielle"},{"last_name":"Szuhai","full_name":"Szuhai, Karoly","first_name":"Karoly"},{"last_name":"van der Wall","full_name":"van der Wall, Elsken","first_name":"Elsken"},{"last_name":"Rueda","full_name":"Rueda, Oscar M.","first_name":"Oscar M."},{"last_name":"Ali","full_name":"Ali, H. Raza","first_name":"H. Raza"},{"last_name":"Caldas","first_name":"Carlos","full_name":"Caldas, Carlos"},{"full_name":"van Diest, Paul J.","first_name":"Paul J.","last_name":"van Diest"},{"orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"},{"full_name":"Sahai, Erik","first_name":"Erik","last_name":"Sahai"},{"last_name":"Derksen","first_name":"Patrick W.B.","full_name":"Derksen, Patrick W.B."}],"day":"22","title":"p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis","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. <i>Nature Communications</i>. 2016;7. doi:<a href=\"https://doi.org/10.1038/ncomms13874\">10.1038/ncomms13874</a>","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. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms13874\">https://doi.org/10.1038/ncomms13874</a>","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).","mla":"van de Ven, Robert A. H., et al. “P120-Catenin Prevents Multinucleation through Control of MKLP1-Dependent RhoA Activity during Cytokinesis.” <i>Nature Communications</i>, vol. 7, 13874, Springer Nature, 2016, doi:<a href=\"https://doi.org/10.1038/ncomms13874\">10.1038/ncomms13874</a>.","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.” <i>Nature Communications</i>. Springer Nature, 2016. <a href=\"https://doi.org/10.1038/ncomms13874\">https://doi.org/10.1038/ncomms13874</a>.","ieee":"R. A. H. van de Ven <i>et al.</i>, “p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis,” <i>Nature Communications</i>, 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."},"doi":"10.1038/ncomms13874","language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"pmid":1,"related_material":{"link":[{"url":"https://doi.org/10.1038/ncomms16030","relation":"erratum"}]}},{"day":"01","author":[{"last_name":"Samanta","full_name":"Samanta, Dipak","first_name":"Dipak"},{"id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","full_name":"Klajn, Rafal","first_name":"Rafal","last_name":"Klajn"}],"type":"journal_article","citation":{"ieee":"D. Samanta and R. Klajn, “Aqueous light-controlled self-assembly of nanoparticles,” <i>Advanced Optical Materials</i>, 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.","chicago":"Samanta, Dipak, and Rafal Klajn. “Aqueous Light-Controlled Self-Assembly of Nanoparticles.” <i>Advanced Optical Materials</i>. Wiley, 2016. <a href=\"https://doi.org/10.1002/adom.201600364\">https://doi.org/10.1002/adom.201600364</a>.","mla":"Samanta, Dipak, and Rafal Klajn. “Aqueous Light-Controlled Self-Assembly of Nanoparticles.” <i>Advanced Optical Materials</i>, vol. 4, no. 9, Wiley, 2016, pp. 1373–77, doi:<a href=\"https://doi.org/10.1002/adom.201600364\">10.1002/adom.201600364</a>.","short":"D. Samanta, R. Klajn, Advanced Optical Materials 4 (2016) 1373–1377.","apa":"Samanta, D., &#38; Klajn, R. (2016). Aqueous light-controlled self-assembly of nanoparticles. <i>Advanced Optical Materials</i>. Wiley. <a href=\"https://doi.org/10.1002/adom.201600364\">https://doi.org/10.1002/adom.201600364</a>","ama":"Samanta D, Klajn R. Aqueous light-controlled self-assembly of nanoparticles. <i>Advanced Optical Materials</i>. 2016;4(9):1373-1377. doi:<a href=\"https://doi.org/10.1002/adom.201600364\">10.1002/adom.201600364</a>"},"title":"Aqueous light-controlled self-assembly of nanoparticles","language":[{"iso":"eng"}],"keyword":["Atomic and Molecular Physics","and Optics","Electronic","Optical and Magnetic Materials"],"doi":"10.1002/adom.201600364","extern":"1","month":"09","date_created":"2023-08-01T09:42:49Z","page":"1373-1377","quality_controlled":"1","publication":"Advanced Optical Materials","status":"public","intvolume":"         4","publisher":"Wiley","article_type":"original","year":"2016","oa_version":"None","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2023-08-07T12:37:53Z","scopus_import":"1","publication_identifier":{"eissn":["2195-1071"]},"abstract":[{"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.","lang":"eng"}],"_id":"13387","date_published":"2016-09-01T00:00:00Z","issue":"9","article_processing_charge":"No","volume":4,"publication_status":"published"},{"publisher":"Wiley","quality_controlled":"1","publication":"ChemPhysChem","intvolume":"        17","status":"public","page":"1711-1711","extern":"1","month":"06","date_created":"2023-08-01T09:43:07Z","language":[{"iso":"eng"}],"keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"doi":"10.1002/cphc.201600480","citation":{"mla":"Udayabhaskararao, T., et al. “Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016).” <i>ChemPhysChem</i>, vol. 17, no. 12, Wiley, 2016, pp. 1711–1711, doi:<a href=\"https://doi.org/10.1002/cphc.201600480\">10.1002/cphc.201600480</a>.","ieee":"T. Udayabhaskararao, P. K. Kundu, J. Ahrens, and R. Klajn, <i>Inside cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem 12/2016)</i>, 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.","chicago":"Udayabhaskararao, T., Pintu K. Kundu, Johannes Ahrens, and Rafal Klajn. <i>Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016)</i>. <i>ChemPhysChem</i>. Vol. 17. Wiley, 2016. <a href=\"https://doi.org/10.1002/cphc.201600480\">https://doi.org/10.1002/cphc.201600480</a>.","apa":"Udayabhaskararao, T., Kundu, P. K., Ahrens, J., &#38; Klajn, R. (2016). <i>Inside cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem 12/2016)</i>. <i>ChemPhysChem</i> (Vol. 17, pp. 1711–1711). Wiley. <a href=\"https://doi.org/10.1002/cphc.201600480\">https://doi.org/10.1002/cphc.201600480</a>","ama":"Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. <i>Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016)</i>. Vol 17. Wiley; 2016:1711-1711. doi:<a href=\"https://doi.org/10.1002/cphc.201600480\">10.1002/cphc.201600480</a>","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."},"title":"Inside cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem 12/2016)","day":"17","author":[{"first_name":"T.","full_name":"Udayabhaskararao, T.","last_name":"Udayabhaskararao"},{"full_name":"Kundu, Pintu K.","first_name":"Pintu K.","last_name":"Kundu"},{"last_name":"Ahrens","full_name":"Ahrens, Johannes","first_name":"Johannes"},{"id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn","first_name":"Rafal","full_name":"Klajn, Rafal"}],"type":"other_academic_publication","publication_status":"published","main_file_link":[{"url":"https://doi.org/10.1002/cphc.201600480","open_access":"1"}],"oa":1,"volume":17,"issue":"12","article_processing_charge":"No","date_published":"2016-06-17T00:00:00Z","_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."}],"date_updated":"2023-08-07T12:43:38Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["1439-4235"],"eissn":["1439-7641"]},"oa_version":"Published Version","year":"2016"},{"publication_identifier":{"eissn":["1439-7641"],"issn":["1439-4235"]},"scopus_import":"1","external_id":{"pmid":["26593975"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2023-08-07T12:46:46Z","oa_version":"None","year":"2016","article_type":"original","volume":17,"publication_status":"published","_id":"13389","date_published":"2016-06-17T00:00:00Z","abstract":[{"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.","lang":"eng"}],"article_processing_charge":"No","issue":"12","doi":"10.1002/cphc.201500897","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"language":[{"iso":"eng"}],"pmid":1,"type":"journal_article","author":[{"last_name":"Udayabhaskararao","first_name":"T.","full_name":"Udayabhaskararao, T."},{"last_name":"Kundu","first_name":"Pintu K.","full_name":"Kundu, Pintu K."},{"first_name":"Johannes","full_name":"Ahrens, Johannes","last_name":"Ahrens"},{"last_name":"Klajn","first_name":"Rafal","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"day":"17","title":"Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters","citation":{"short":"T. Udayabhaskararao, P.K. Kundu, J. Ahrens, R. Klajn, ChemPhysChem 17 (2016) 1805–1809.","apa":"Udayabhaskararao, T., Kundu, P. K., Ahrens, J., &#38; Klajn, R. (2016). Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters. <i>ChemPhysChem</i>. Wiley. <a href=\"https://doi.org/10.1002/cphc.201500897\">https://doi.org/10.1002/cphc.201500897</a>","ama":"Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters. <i>ChemPhysChem</i>. 2016;17(12):1805-1809. doi:<a href=\"https://doi.org/10.1002/cphc.201500897\">10.1002/cphc.201500897</a>","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.","ieee":"T. Udayabhaskararao, P. K. Kundu, J. Ahrens, and R. Klajn, “Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters,” <i>ChemPhysChem</i>, vol. 17, no. 12. Wiley, pp. 1805–1809, 2016.","chicago":"Udayabhaskararao, T., Pintu K. Kundu, Johannes Ahrens, and Rafal Klajn. “Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters.” <i>ChemPhysChem</i>. Wiley, 2016. <a href=\"https://doi.org/10.1002/cphc.201500897\">https://doi.org/10.1002/cphc.201500897</a>.","mla":"Udayabhaskararao, T., et al. “Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters.” <i>ChemPhysChem</i>, vol. 17, no. 12, Wiley, 2016, pp. 1805–09, doi:<a href=\"https://doi.org/10.1002/cphc.201500897\">10.1002/cphc.201500897</a>."},"intvolume":"        17","status":"public","publication":"ChemPhysChem","quality_controlled":"1","publisher":"Wiley","date_created":"2023-08-01T09:43:18Z","month":"06","extern":"1","page":"1805-1809"}]