[{"publication_status":"published","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."}],"external_id":{"unknown":["31135340"]},"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"ddc":["580"],"quality_controlled":"1","volume":8,"department":[{"_id":"XiFe"}],"extern":"1","date_published":"2019-05-28T00:00:00Z","publisher":"eLife Sciences Publications, Ltd","keyword":["General Immunology and Microbiology","General Biochemistry","Genetics and Molecular Biology","General Medicine","General Neuroscience"],"date_created":"2023-01-16T09:17:21Z","citation":{"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>","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>.","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>.","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.","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>","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.","short":"S. He, M. Vickers, J. Zhang, X. Feng, ELife 8 (2019)."},"year":"2019","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_type":"original","_id":"12192","file_date_updated":"2023-02-07T09:42:46Z","doi":"10.7554/elife.42530","author":[{"full_name":"He, Shengbo","first_name":"Shengbo","last_name":"He"},{"last_name":"Vickers","full_name":"Vickers, Martin","first_name":"Martin"},{"last_name":"Zhang","full_name":"Zhang, Jingyi","first_name":"Jingyi"},{"first_name":"Xiaoqi","full_name":"Feng, Xiaoqi","orcid":"0000-0002-4008-1234","id":"e0164712-22ee-11ed-b12a-d80fcdf35958","last_name":"Feng"}],"file":[{"date_created":"2023-02-07T09:42:46Z","date_updated":"2023-02-07T09:42:46Z","success":1,"checksum":"ea6b89c20d59e5eb3646916fe5d568ad","file_id":"12525","file_name":"2019_elife_He.pdf","relation":"main_file","access_level":"open_access","file_size":2493837,"content_type":"application/pdf","creator":"alisjak"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","main_file_link":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6594752/","open_access":"1"}],"oa_version":"Published Version","day":"28","publication_identifier":{"issn":["2050-084X"]},"month":"05","status":"public","type":"journal_article","title":"Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation","article_processing_charge":"No","date_updated":"2023-05-08T10:54:12Z","oa":1,"scopus_import":"1","intvolume":"         8","has_accepted_license":"1","language":[{"iso":"eng"}],"publication":"eLife"},{"publication_status":"published","abstract":[{"text":"Atomic-resolution structure determination is crucial for understanding protein function. Cryo-EM and NMR spectroscopy both provide structural information, but currently cryo-EM does not routinely give access to atomic-level structural data, and, generally, NMR structure determination is restricted to small (<30 kDa) proteins. We introduce an integrated structure determination approach that simultaneously uses NMR and EM data to overcome the limits of each of these methods. The approach enables structure determination of the 468 kDa large dodecameric aminopeptidase TET2 to a precision and accuracy below 1 Å by combining secondary-structure information obtained from near-complete magic-angle-spinning NMR assignments of the 39 kDa-large subunits, distance restraints from backbone amides and ILV methyl groups, and a 4.1 Å resolution EM map. The resulting structure exceeds current standards of NMR and EM structure determination in terms of molecular weight and precision. Importantly, the approach is successful even in cases where only medium-resolution cryo-EM data are available.","lang":"eng"}],"external_id":{"pmid":["31217444"]},"volume":10,"quality_controlled":"1","extern":"1","date_published":"2019-06-19T00:00:00Z","publisher":"Springer Nature","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"citation":{"ama":"Gauto DF, Estrozi LF, Schwieters CD, et al. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. <i>Nature Communications</i>. 2019;10. doi:<a href=\"https://doi.org/10.1038/s41467-019-10490-9\">10.1038/s41467-019-10490-9</a>","ieee":"D. F. Gauto <i>et al.</i>, “Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex,” <i>Nature Communications</i>, vol. 10. Springer Nature, 2019.","short":"D.F. Gauto, L.F. Estrozi, C.D. Schwieters, G. Effantin, P. Macek, R. Sounier, A.C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Güntert, A. Favier, G. Schoehn, P. Schanda, J. Boisbouvier, Nature Communications 10 (2019).","ista":"Gauto DF, Estrozi LF, Schwieters CD, Effantin G, Macek P, Sounier R, Sivertsen AC, Schmidt E, Kerfah R, Mas G, Colletier J-P, Güntert P, Favier A, Schoehn G, Schanda P, Boisbouvier J. 2019. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. 10, 2697.","chicago":"Gauto, Diego F., Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin, Pavel Macek, Remy Sounier, Astrid C. Sivertsen, et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.” <i>Nature Communications</i>. Springer Nature, 2019. <a href=\"https://doi.org/10.1038/s41467-019-10490-9\">https://doi.org/10.1038/s41467-019-10490-9</a>.","mla":"Gauto, Diego F., et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.” <i>Nature Communications</i>, vol. 10, 2697, Springer Nature, 2019, doi:<a href=\"https://doi.org/10.1038/s41467-019-10490-9\">10.1038/s41467-019-10490-9</a>.","apa":"Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., … Boisbouvier, J. (2019). Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-019-10490-9\">https://doi.org/10.1038/s41467-019-10490-9</a>"},"date_created":"2020-09-17T10:28:25Z","year":"2019","article_number":"2697","_id":"8405","article_type":"original","doi":"10.1038/s41467-019-10490-9","author":[{"last_name":"Gauto","first_name":"Diego F.","full_name":"Gauto, Diego F."},{"last_name":"Estrozi","full_name":"Estrozi, Leandro F.","first_name":"Leandro F."},{"full_name":"Schwieters, Charles D.","first_name":"Charles D.","last_name":"Schwieters"},{"full_name":"Effantin, Gregory","first_name":"Gregory","last_name":"Effantin"},{"last_name":"Macek","first_name":"Pavel","full_name":"Macek, Pavel"},{"full_name":"Sounier, Remy","first_name":"Remy","last_name":"Sounier"},{"last_name":"Sivertsen","first_name":"Astrid C.","full_name":"Sivertsen, Astrid C."},{"last_name":"Schmidt","full_name":"Schmidt, Elena","first_name":"Elena"},{"last_name":"Kerfah","full_name":"Kerfah, Rime","first_name":"Rime"},{"first_name":"Guillaume","full_name":"Mas, Guillaume","last_name":"Mas"},{"full_name":"Colletier, Jacques-Philippe","first_name":"Jacques-Philippe","last_name":"Colletier"},{"last_name":"Güntert","full_name":"Güntert, Peter","first_name":"Peter"},{"full_name":"Favier, Adrien","first_name":"Adrien","last_name":"Favier"},{"last_name":"Schoehn","full_name":"Schoehn, Guy","first_name":"Guy"},{"orcid":"0000-0002-9350-7606","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul"},{"first_name":"Jerome","full_name":"Boisbouvier, Jerome","last_name":"Boisbouvier"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","main_file_link":[{"url":"https://doi.org/10.1038/s41467-019-10490-9","open_access":"1"}],"day":"19","oa_version":"Published Version","month":"06","publication_identifier":{"issn":["2041-1723"]},"status":"public","type":"journal_article","pmid":1,"title":"Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex","article_processing_charge":"No","date_updated":"2021-01-12T08:19:03Z","oa":1,"intvolume":"        10","language":[{"iso":"eng"}],"publication":"Nature Communications"},{"publication_status":"published","external_id":{"pmid":["31543461"]},"abstract":[{"text":"Anti-silencing function 1 (ASF1) is a conserved H3-H4 histone chaperone involved in histone dynamics during replication, transcription, and DNA repair. Overexpressed in proliferating tissues including many tumors, ASF1 has emerged as a promising therapeutic target. Here, we combine structural, computational, and biochemical approaches to design peptides that inhibit the ASF1-histone interaction. Starting from the structure of the human ASF1-histone complex, we developed a rational design strategy combining epitope tethering and optimization of interface contacts to identify a potent peptide inhibitor with a dissociation constant of 3 nM. When introduced into cultured cells, the inhibitors impair cell proliferation, perturb cell-cycle progression, and reduce cell migration and invasion in a manner commensurate with their affinity for ASF1. Finally, we find that direct injection of the most potent ASF1 peptide inhibitor in mouse allografts reduces tumor growth. Our results open new avenues to use ASF1 inhibitors as promising leads for cancer therapy.","lang":"eng"}],"extern":"1","page":"1573-1585.e10","volume":26,"quality_controlled":"1","publisher":"Elsevier","date_published":"2019-11-21T00:00:00Z","citation":{"apa":"Bakail, M. M., Gaubert, A., Andreani, J., Moal, G., Pinna, G., Boyarchuk, E., … Ochsenbein, F. (2019). Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1. <i>Cell Chemical Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.chembiol.2019.09.002\">https://doi.org/10.1016/j.chembiol.2019.09.002</a>","chicago":"Bakail, May M, Albane Gaubert, Jessica Andreani, Gwenaëlle Moal, Guillaume Pinna, Ekaterina Boyarchuk, Marie-Cécile Gaillard, et al. “Design on a Rational Basis of High-Affinity Peptides Inhibiting the Histone Chaperone ASF1.” <i>Cell Chemical Biology</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.chembiol.2019.09.002\">https://doi.org/10.1016/j.chembiol.2019.09.002</a>.","mla":"Bakail, May M., et al. “Design on a Rational Basis of High-Affinity Peptides Inhibiting the Histone Chaperone ASF1.” <i>Cell Chemical Biology</i>, vol. 26, no. 11, Elsevier, 2019, p. 1573–1585.e10, doi:<a href=\"https://doi.org/10.1016/j.chembiol.2019.09.002\">10.1016/j.chembiol.2019.09.002</a>.","ista":"Bakail MM, Gaubert A, Andreani J, Moal G, Pinna G, Boyarchuk E, Gaillard M-C, Courbeyrette R, Mann C, Thuret J-Y, Guichard B, Murciano B, Richet N, Poitou A, Frederic C, Le Du M-H, Agez M, Roelants C, Gurard-Levin ZA, Almouzni G, Cherradi N, Guerois R, Ochsenbein F. 2019. Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1. Cell Chemical Biology. 26(11), 1573–1585.e10.","ieee":"M. M. Bakail <i>et al.</i>, “Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1,” <i>Cell Chemical Biology</i>, vol. 26, no. 11. Elsevier, p. 1573–1585.e10, 2019.","ama":"Bakail MM, Gaubert A, Andreani J, et al. Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1. <i>Cell Chemical Biology</i>. 2019;26(11):1573-1585.e10. doi:<a href=\"https://doi.org/10.1016/j.chembiol.2019.09.002\">10.1016/j.chembiol.2019.09.002</a>","short":"M.M. Bakail, A. Gaubert, J. Andreani, G. Moal, G. Pinna, E. Boyarchuk, M.-C. Gaillard, R. Courbeyrette, C. Mann, J.-Y. Thuret, B. Guichard, B. Murciano, N. Richet, A. Poitou, C. Frederic, M.-H. Le Du, M. Agez, C. Roelants, Z.A. Gurard-Levin, G. Almouzni, N. Cherradi, R. Guerois, F. Ochsenbein, Cell Chemical Biology 26 (2019) 1573–1585.e10."},"date_created":"2021-01-19T11:04:50Z","keyword":["Clinical Biochemistry","Molecular Medicine","Biochemistry","Molecular Biology","Pharmacology","Drug Discovery"],"year":"2019","article_type":"original","_id":"9018","doi":"10.1016/j.chembiol.2019.09.002","author":[{"orcid":"0000-0002-9592-1587","last_name":"Bakail","id":"FB3C3F8E-522F-11EA-B186-22963DDC885E","first_name":"May M","full_name":"Bakail, May M"},{"last_name":"Gaubert","first_name":"Albane","full_name":"Gaubert, Albane"},{"full_name":"Andreani, Jessica","first_name":"Jessica","last_name":"Andreani"},{"last_name":"Moal","full_name":"Moal, Gwenaëlle","first_name":"Gwenaëlle"},{"first_name":"Guillaume","full_name":"Pinna, Guillaume","last_name":"Pinna"},{"last_name":"Boyarchuk","full_name":"Boyarchuk, Ekaterina","first_name":"Ekaterina"},{"full_name":"Gaillard, Marie-Cécile","first_name":"Marie-Cécile","last_name":"Gaillard"},{"last_name":"Courbeyrette","first_name":"Regis","full_name":"Courbeyrette, Regis"},{"full_name":"Mann, Carl","first_name":"Carl","last_name":"Mann"},{"last_name":"Thuret","first_name":"Jean-Yves","full_name":"Thuret, Jean-Yves"},{"last_name":"Guichard","full_name":"Guichard, Bérengère","first_name":"Bérengère"},{"last_name":"Murciano","full_name":"Murciano, Brice","first_name":"Brice"},{"full_name":"Richet, Nicolas","first_name":"Nicolas","last_name":"Richet"},{"full_name":"Poitou, Adeline","first_name":"Adeline","last_name":"Poitou"},{"last_name":"Frederic","first_name":"Claire","full_name":"Frederic, Claire"},{"last_name":"Le Du","first_name":"Marie-Hélène","full_name":"Le Du, Marie-Hélène"},{"last_name":"Agez","first_name":"Morgane","full_name":"Agez, Morgane"},{"last_name":"Roelants","full_name":"Roelants, Caroline","first_name":"Caroline"},{"first_name":"Zachary A.","full_name":"Gurard-Levin, Zachary A.","last_name":"Gurard-Levin"},{"full_name":"Almouzni, Geneviève","first_name":"Geneviève","last_name":"Almouzni"},{"last_name":"Cherradi","first_name":"Nadia","full_name":"Cherradi, Nadia"},{"first_name":"Raphael","full_name":"Guerois, Raphael","last_name":"Guerois"},{"last_name":"Ochsenbein","first_name":"Françoise","full_name":"Ochsenbein, Françoise"}],"oa_version":"Published Version","day":"21","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.chembiol.2019.09.002"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["2451-9456"]},"month":"11","pmid":1,"type":"journal_article","status":"public","title":"Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1","date_updated":"2023-02-23T13:46:53Z","oa":1,"article_processing_charge":"No","issue":"11","intvolume":"        26","language":[{"iso":"eng"}],"publication":"Cell Chemical Biology"},{"month":"07","publication_identifier":{"issn":["2041-1723"]},"file":[{"creator":"cziletti","access_level":"open_access","relation":"main_file","file_size":2820337,"content_type":"application/pdf","success":1,"checksum":"70c6e5d6fbea0932b0669505ab6633ec","file_name":"2019_NatureComm_Ramananarivo.pdf","file_id":"9061","date_created":"2021-02-02T13:47:21Z","date_updated":"2021-02-02T13:47:21Z"}],"user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","day":"29","oa_version":"Published Version","arxiv":1,"author":[{"last_name":"Ramananarivo","first_name":"Sophie","full_name":"Ramananarivo, Sophie"},{"full_name":"Ducrot, Etienne","first_name":"Etienne","last_name":"Ducrot"},{"orcid":"0000-0002-7253-9465","id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d","last_name":"Palacci","first_name":"Jérémie A","full_name":"Palacci, Jérémie A"}],"status":"public","type":"journal_article","pmid":1,"scopus_import":"1","has_accepted_license":"1","intvolume":"        10","issue":"1","article_processing_charge":"No","date_updated":"2023-02-23T13:47:59Z","oa":1,"title":"Activity-controlled annealing of colloidal monolayers","publication":"Nature Communications","language":[{"iso":"eng"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"ddc":["530"],"abstract":[{"lang":"eng","text":"Molecular motors are essential to the living, generating fluctuations that boost transport and assist assembly. Active colloids, that consume energy to move, hold similar potential for man-made materials controlled by forces generated from within. Yet, their use as a powerhouse in materials science lacks. Here we show a massive acceleration of the annealing of a monolayer of passive beads by moderate addition of self-propelled microparticles. We rationalize our observations with a model of collisions that drive active fluctuations and activate the annealing. The experiment is quantitatively compared with Brownian dynamic simulations that further unveil a dynamical transition in the mechanism of annealing. Active dopants travel uniformly in the system or co-localize at the grain boundaries as a result of the persistence of their motion. Our findings uncover the potential of internal activity to control materials and lay the groundwork for the rise of materials science beyond equilibrium."}],"external_id":{"arxiv":["1909.07382"],"pmid":["31358762"]},"publication_status":"published","date_published":"2019-07-29T00:00:00Z","publisher":"Springer Nature","quality_controlled":"1","volume":10,"extern":"1","article_number":"3380","year":"2019","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"date_created":"2021-02-02T13:43:36Z","citation":{"apa":"Ramananarivo, S., Ducrot, E., &#38; Palacci, J. A. (2019). Activity-controlled annealing of colloidal monolayers. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-019-11362-y\">https://doi.org/10.1038/s41467-019-11362-y</a>","short":"S. Ramananarivo, E. Ducrot, J.A. Palacci, Nature Communications 10 (2019).","ieee":"S. Ramananarivo, E. Ducrot, and J. A. Palacci, “Activity-controlled annealing of colloidal monolayers,” <i>Nature Communications</i>, vol. 10, no. 1. Springer Nature, 2019.","ama":"Ramananarivo S, Ducrot E, Palacci JA. Activity-controlled annealing of colloidal monolayers. <i>Nature Communications</i>. 2019;10(1). doi:<a href=\"https://doi.org/10.1038/s41467-019-11362-y\">10.1038/s41467-019-11362-y</a>","chicago":"Ramananarivo, Sophie, Etienne Ducrot, and Jérémie A Palacci. “Activity-Controlled Annealing of Colloidal Monolayers.” <i>Nature Communications</i>. Springer Nature, 2019. <a href=\"https://doi.org/10.1038/s41467-019-11362-y\">https://doi.org/10.1038/s41467-019-11362-y</a>.","mla":"Ramananarivo, Sophie, et al. “Activity-Controlled Annealing of Colloidal Monolayers.” <i>Nature Communications</i>, vol. 10, no. 1, 3380, Springer Nature, 2019, doi:<a href=\"https://doi.org/10.1038/s41467-019-11362-y\">10.1038/s41467-019-11362-y</a>.","ista":"Ramananarivo S, Ducrot E, Palacci JA. 2019. Activity-controlled annealing of colloidal monolayers. Nature Communications. 10(1), 3380."},"doi":"10.1038/s41467-019-11362-y","article_type":"original","_id":"9060","file_date_updated":"2021-02-02T13:47:21Z"},{"abstract":[{"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.","lang":"eng"}],"external_id":{"pmid":["31226513"]},"publication_status":"published","date_published":"2019-06-18T00:00:00Z","publisher":"Elsevier","volume":58,"quality_controlled":"1","extern":"1","page":"43-52","year":"2019","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.","keyword":["molecular biology","structural biology"],"citation":{"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>","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>.","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>.","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.","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>","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.","short":"A.E. Hafner, J. Krausser, A. Šarić, Current Opinion in Structural Biology 58 (2019) 43–52."},"date_created":"2021-11-26T11:33:21Z","doi":"10.1016/j.sbi.2019.05.018","_id":"10355","article_type":"original","publication_identifier":{"issn":["0959-440X"]},"month":"06","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","oa_version":"Preprint","main_file_link":[{"url":"https://arxiv.org/abs/1906.09349","open_access":"1"}],"day":"18","author":[{"last_name":"Hafner","first_name":"Anne E","full_name":"Hafner, Anne E"},{"last_name":"Krausser","first_name":"Johannes","full_name":"Krausser, Johannes"},{"orcid":"0000-0002-7854-2139","last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","first_name":"Anđela","full_name":"Šarić, Anđela"}],"type":"journal_article","status":"public","pmid":1,"scopus_import":"1","intvolume":"        58","article_processing_charge":"No","date_updated":"2021-11-26T11:54:25Z","oa":1,"title":"Minimal coarse-grained models for molecular self-organisation in biology","publication":"Current Opinion in Structural Biology","language":[{"iso":"eng"}]},{"publication":"Nature Reviews Genetics","language":[{"iso":"eng"}],"scopus_import":"1","intvolume":"        20","article_processing_charge":"No","issue":"1","date_updated":"2022-07-18T08:31:42Z","title":"Coaching from the sidelines: The nuclear periphery in genome regulation","type":"journal_article","status":"public","pmid":1,"month":"01","publication_identifier":{"issn":["1471-0056"],"eissn":["1471-0064"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","day":"01","oa_version":"None","author":[{"full_name":"Buchwalter, Abigail","first_name":"Abigail","last_name":"Buchwalter"},{"last_name":"Kaneshiro","full_name":"Kaneshiro, Jeanae M.","first_name":"Jeanae M."},{"orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W"}],"doi":"10.1038/s41576-018-0063-5","article_type":"review","_id":"11059","year":"2019","keyword":["Genetics (clinical)","Genetics","Molecular Biology"],"date_created":"2022-04-07T07:44:45Z","citation":{"apa":"Buchwalter, A., Kaneshiro, J. M., &#38; Hetzer, M. (2019). Coaching from the sidelines: The nuclear periphery in genome regulation. <i>Nature Reviews Genetics</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41576-018-0063-5\">https://doi.org/10.1038/s41576-018-0063-5</a>","mla":"Buchwalter, Abigail, et al. “Coaching from the Sidelines: The Nuclear Periphery in Genome Regulation.” <i>Nature Reviews Genetics</i>, vol. 20, no. 1, Springer Nature, 2019, pp. 39–50, doi:<a href=\"https://doi.org/10.1038/s41576-018-0063-5\">10.1038/s41576-018-0063-5</a>.","ista":"Buchwalter A, Kaneshiro JM, Hetzer M. 2019. Coaching from the sidelines: The nuclear periphery in genome regulation. Nature Reviews Genetics. 20(1), 39–50.","chicago":"Buchwalter, Abigail, Jeanae M. Kaneshiro, and Martin Hetzer. “Coaching from the Sidelines: The Nuclear Periphery in Genome Regulation.” <i>Nature Reviews Genetics</i>. Springer Nature, 2019. <a href=\"https://doi.org/10.1038/s41576-018-0063-5\">https://doi.org/10.1038/s41576-018-0063-5</a>.","short":"A. Buchwalter, J.M. Kaneshiro, M. Hetzer, Nature Reviews Genetics 20 (2019) 39–50.","ieee":"A. Buchwalter, J. M. Kaneshiro, and M. Hetzer, “Coaching from the sidelines: The nuclear periphery in genome regulation,” <i>Nature Reviews Genetics</i>, vol. 20, no. 1. Springer Nature, pp. 39–50, 2019.","ama":"Buchwalter A, Kaneshiro JM, Hetzer M. Coaching from the sidelines: The nuclear periphery in genome regulation. <i>Nature Reviews Genetics</i>. 2019;20(1):39-50. doi:<a href=\"https://doi.org/10.1038/s41576-018-0063-5\">10.1038/s41576-018-0063-5</a>"},"date_published":"2019-01-01T00:00:00Z","publisher":"Springer Nature","quality_controlled":"1","volume":20,"page":"39-50","extern":"1","abstract":[{"lang":"eng","text":"The genome is packaged and organized nonrandomly within the 3D space of the nucleus to promote efficient gene expression and to faithfully maintain silencing of heterochromatin. The genome is enclosed within the nucleus by the nuclear envelope membrane, which contains a set of proteins that actively participate in chromatin organization and gene regulation. Technological advances are providing views of genome organization at unprecedented resolution and are beginning to reveal the ways that cells co-opt the structures of the nuclear periphery for nuclear organization and gene regulation. These genome regulatory roles of proteins of the nuclear periphery have important influences on development, disease and ageing."}],"external_id":{"pmid":["30356165"]},"publication_status":"published"},{"pmid":1,"type":"journal_article","status":"public","author":[{"first_name":"Abigail","full_name":"Buchwalter, Abigail","last_name":"Buchwalter"},{"last_name":"Schulte","full_name":"Schulte, Roberta","first_name":"Roberta"},{"first_name":"Hsiao","full_name":"Tsai, Hsiao","last_name":"Tsai"},{"last_name":"Capitanio","full_name":"Capitanio, Juliana","first_name":"Juliana"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W"}],"publication_identifier":{"issn":["2050-084X"]},"month":"10","day":"10","oa_version":"Published Version","file":[{"file_name":"2019_eLife_Buchwalter.pdf","file_id":"11138","checksum":"1e8672a1e9c3dc0a2d3d0dad89673616","success":1,"date_updated":"2022-04-08T08:18:01Z","date_created":"2022-04-08T08:18:01Z","creator":"dernst","content_type":"application/pdf","access_level":"open_access","relation":"main_file","file_size":6984654}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","language":[{"iso":"eng"}],"publication":"eLife","date_updated":"2023-05-31T06:36:22Z","oa":1,"article_processing_charge":"No","title":"Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress","intvolume":"         8","has_accepted_license":"1","scopus_import":"1","publisher":"eLife Sciences Publications","date_published":"2019-10-10T00:00:00Z","extern":"1","volume":8,"quality_controlled":"1","publication_status":"published","ddc":["570"],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"external_id":{"pmid":["31599721"]},"abstract":[{"lang":"eng","text":"The inner nuclear membrane (INM) is a subdomain of the endoplasmic reticulum (ER) that is gated by the nuclear pore complex. It is unknown whether proteins of the INM and ER are degraded through shared or distinct pathways in mammalian cells. We applied dynamic proteomics to profile protein half-lives and report that INM and ER residents turn over at similar rates, indicating that the INM’s unique topology is not a barrier to turnover. Using a microscopy approach, we observed that the proteasome can degrade INM proteins in situ. However, we also uncovered evidence for selective, vesicular transport-mediated turnover of a single INM protein, emerin, that is potentiated by ER stress. Emerin is rapidly cleared from the INM by a mechanism that requires emerin’s LEM domain to mediate vesicular trafficking to lysosomes. This work demonstrates that the INM can be dynamically remodeled in response to environmental inputs."}],"file_date_updated":"2022-04-08T08:18:01Z","_id":"11060","article_type":"original","doi":"10.7554/elife.49796","year":"2019","citation":{"apa":"Buchwalter, A., Schulte, R., Tsai, H., Capitanio, J., &#38; Hetzer, M. (2019). Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/elife.49796\">https://doi.org/10.7554/elife.49796</a>","mla":"Buchwalter, Abigail, et al. “Selective Clearance of the Inner Nuclear Membrane Protein Emerin by Vesicular Transport during ER Stress.” <i>ELife</i>, vol. 8, e49796, eLife Sciences Publications, 2019, doi:<a href=\"https://doi.org/10.7554/elife.49796\">10.7554/elife.49796</a>.","ista":"Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. 2019. Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. eLife. 8, e49796.","chicago":"Buchwalter, Abigail, Roberta Schulte, Hsiao Tsai, Juliana Capitanio, and Martin Hetzer. “Selective Clearance of the Inner Nuclear Membrane Protein Emerin by Vesicular Transport during ER Stress.” <i>ELife</i>. eLife Sciences Publications, 2019. <a href=\"https://doi.org/10.7554/elife.49796\">https://doi.org/10.7554/elife.49796</a>.","ieee":"A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, and M. Hetzer, “Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress,” <i>eLife</i>, vol. 8. eLife Sciences Publications, 2019.","ama":"Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. <i>eLife</i>. 2019;8. doi:<a href=\"https://doi.org/10.7554/elife.49796\">10.7554/elife.49796</a>","short":"A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, M. Hetzer, ELife 8 (2019)."},"date_created":"2022-04-07T07:45:02Z","keyword":["General Immunology and Microbiology","General Biochemistry","Genetics and Molecular Biology","General Medicine","General Neuroscience"],"related_material":{"record":[{"status":"public","relation":"research_data","id":"13079"}]},"article_number":"e49796"},{"pmid":1,"status":"public","type":"journal_article","author":[{"full_name":"Arrojo e Drigo, Rafael","first_name":"Rafael","last_name":"Arrojo e Drigo"},{"full_name":"Lev-Ram, Varda","first_name":"Varda","last_name":"Lev-Ram"},{"last_name":"Tyagi","full_name":"Tyagi, Swati","first_name":"Swati"},{"first_name":"Ranjan","full_name":"Ramachandra, Ranjan","last_name":"Ramachandra"},{"full_name":"Deerinck, Thomas","first_name":"Thomas","last_name":"Deerinck"},{"last_name":"Bushong","full_name":"Bushong, Eric","first_name":"Eric"},{"first_name":"Sebastien","full_name":"Phan, Sebastien","last_name":"Phan"},{"first_name":"Victoria","full_name":"Orphan, Victoria","last_name":"Orphan"},{"full_name":"Lechene, Claude","first_name":"Claude","last_name":"Lechene"},{"full_name":"Ellisman, Mark H.","first_name":"Mark H.","last_name":"Ellisman"},{"orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","first_name":"Martin W"}],"oa_version":"Published Version","day":"06","main_file_link":[{"url":"https://doi.org/10.1016/j.cmet.2019.05.010","open_access":"1"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","month":"08","publication_identifier":{"issn":["1550-4131"]},"language":[{"iso":"eng"}],"publication":"Cell Metabolism","title":"Age mosaicism across multiple scales in adult tissues","oa":1,"date_updated":"2022-07-18T08:32:30Z","article_processing_charge":"No","issue":"2","scopus_import":"1","intvolume":"        30","extern":"1","page":"343-351.e3","quality_controlled":"1","volume":30,"publisher":"Elsevier","date_published":"2019-08-06T00:00:00Z","publication_status":"published","external_id":{"pmid":["31178361"]},"abstract":[{"lang":"eng","text":"Most neurons are not replaced during an animal’s lifetime. This nondividing state is characterized by extreme longevity and age-dependent decline of key regulatory proteins. To study the lifespans of cells and proteins in adult tissues, we combined isotope labeling of mice with a hybrid imaging method (MIMS-EM). Using 15N mapping, we show that liver and pancreas are composed of cells with vastly different ages, many as old as the animal. Strikingly, we also found that a subset of fibroblasts and endothelial cells, both known for their replicative potential, are characterized by the absence of cell division during adulthood. In addition, we show that the primary cilia of beta cells and neurons contains different structural regions with vastly different lifespans. Based on these results, we propose that age mosaicism across multiple scales is a fundamental principle of adult tissue, cell, and protein complex organization."}],"article_type":"original","_id":"11062","doi":"10.1016/j.cmet.2019.05.010","citation":{"ieee":"R. Arrojo e Drigo <i>et al.</i>, “Age mosaicism across multiple scales in adult tissues,” <i>Cell Metabolism</i>, vol. 30, no. 2. Elsevier, p. 343–351.e3, 2019.","ama":"Arrojo e Drigo R, Lev-Ram V, Tyagi S, et al. Age mosaicism across multiple scales in adult tissues. <i>Cell Metabolism</i>. 2019;30(2):343-351.e3. doi:<a href=\"https://doi.org/10.1016/j.cmet.2019.05.010\">10.1016/j.cmet.2019.05.010</a>","short":"R. Arrojo e Drigo, V. Lev-Ram, S. Tyagi, R. Ramachandra, T. Deerinck, E. Bushong, S. Phan, V. Orphan, C. Lechene, M.H. Ellisman, M. Hetzer, Cell Metabolism 30 (2019) 343–351.e3.","ista":"Arrojo e Drigo R, Lev-Ram V, Tyagi S, Ramachandra R, Deerinck T, Bushong E, Phan S, Orphan V, Lechene C, Ellisman MH, Hetzer M. 2019. Age mosaicism across multiple scales in adult tissues. Cell Metabolism. 30(2), 343–351.e3.","chicago":"Arrojo e Drigo, Rafael, Varda Lev-Ram, Swati Tyagi, Ranjan Ramachandra, Thomas Deerinck, Eric Bushong, Sebastien Phan, et al. “Age Mosaicism across Multiple Scales in Adult Tissues.” <i>Cell Metabolism</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.cmet.2019.05.010\">https://doi.org/10.1016/j.cmet.2019.05.010</a>.","mla":"Arrojo e Drigo, Rafael, et al. “Age Mosaicism across Multiple Scales in Adult Tissues.” <i>Cell Metabolism</i>, vol. 30, no. 2, Elsevier, 2019, p. 343–351.e3, doi:<a href=\"https://doi.org/10.1016/j.cmet.2019.05.010\">10.1016/j.cmet.2019.05.010</a>.","apa":"Arrojo e Drigo, R., Lev-Ram, V., Tyagi, S., Ramachandra, R., Deerinck, T., Bushong, E., … Hetzer, M. (2019). Age mosaicism across multiple scales in adult tissues. <i>Cell Metabolism</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cmet.2019.05.010\">https://doi.org/10.1016/j.cmet.2019.05.010</a>"},"date_created":"2022-04-07T07:45:21Z","keyword":["Cell Biology","Molecular Biology","Physiology"],"year":"2019"},{"intvolume":"       175","date_updated":"2021-01-12T08:19:15Z","issue":"5","year":"2018","article_processing_charge":"No","citation":{"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.","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>","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."},"title":"Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space","date_created":"2020-09-18T10:04:39Z","keyword":["General Biochemistry","Genetics and Molecular Biology"],"publication":"Cell","doi":"10.1016/j.cell.2018.10.039","article_type":"original","_id":"8436","language":[{"iso":"eng"}],"publication_identifier":{"issn":["0092-8674"]},"month":"11","day":"15","oa_version":"None","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","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."}],"author":[{"last_name":"Weinhäupl","full_name":"Weinhäupl, Katharina","first_name":"Katharina"},{"full_name":"Lindau, Caroline","first_name":"Caroline","last_name":"Lindau"},{"first_name":"Audrey","full_name":"Hessel, Audrey","last_name":"Hessel"},{"full_name":"Wang, Yong","first_name":"Yong","last_name":"Wang"},{"last_name":"Schütze","full_name":"Schütze, Conny","first_name":"Conny"},{"last_name":"Jores","full_name":"Jores, Tobias","first_name":"Tobias"},{"full_name":"Melchionda, Laura","first_name":"Laura","last_name":"Melchionda"},{"last_name":"Schönfisch","full_name":"Schönfisch, Birgit","first_name":"Birgit"},{"last_name":"Kalbacher","first_name":"Hubert","full_name":"Kalbacher, Hubert"},{"full_name":"Bersch, Beate","first_name":"Beate","last_name":"Bersch"},{"last_name":"Rapaport","full_name":"Rapaport, Doron","first_name":"Doron"},{"first_name":"Martha","full_name":"Brennich, Martha","last_name":"Brennich"},{"first_name":"Kresten","full_name":"Lindorff-Larsen, Kresten","last_name":"Lindorff-Larsen"},{"last_name":"Wiedemann","full_name":"Wiedemann, Nils","first_name":"Nils"},{"orcid":"0000-0002-9350-7606","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","first_name":"Paul"}],"publication_status":"published","publisher":"Elsevier","date_published":"2018-11-15T00:00:00Z","status":"public","type":"journal_article","extern":"1","page":"1365-1379.e25","volume":175,"quality_controlled":"1"},{"publication":"Nature Structural & Molecular Biology","doi":"10.1038/s41594-018-0127-4","language":[{"iso":"eng"}],"_id":"8438","article_type":"letter_note","intvolume":"        25","date_updated":"2021-01-12T08:19:16Z","issue":"9","year":"2018","article_processing_charge":"No","date_created":"2020-09-18T10:04:59Z","title":"Dynamics and interactions of AAC3 in DPC are not functionally relevant","citation":{"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>","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.","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>.","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>.","short":"V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature Structural &#38; Molecular Biology 25 (2018) 745–747.","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>","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."},"keyword":["Molecular Biology","Structural Biology"],"publisher":"Springer Nature","date_published":"2018-09-03T00:00:00Z","type":"journal_article","status":"public","extern":"1","page":"745-747","quality_controlled":"1","volume":25,"publication_identifier":{"issn":["1545-9993","1545-9985"]},"month":"09","oa_version":"None","day":"03","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"first_name":"Vilius","full_name":"Kurauskas, Vilius","last_name":"Kurauskas"},{"last_name":"Hessel","full_name":"Hessel, Audrey","first_name":"Audrey"},{"first_name":"François","full_name":"Dehez, François","last_name":"Dehez"},{"last_name":"Chipot","full_name":"Chipot, Christophe","first_name":"Christophe"},{"last_name":"Bersch","full_name":"Bersch, Beate","first_name":"Beate"},{"full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"}],"publication_status":"published"},{"publication":"Journal of Biological Chemistry","doi":"10.1074/jbc.ra118.002251","language":[{"iso":"eng"}],"_id":"8440","article_type":"original","intvolume":"       293","issue":"22","year":"2018","article_processing_charge":"No","date_updated":"2021-01-12T08:19:17Z","keyword":["Cell Biology","Biochemistry","Molecular Biology"],"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.","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.","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.","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>","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>"},"title":"The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis","date_created":"2020-09-18T10:05:18Z","date_published":"2018-06-01T00:00:00Z","type":"journal_article","status":"public","publisher":"American Society for Biochemistry & Molecular Biology","quality_controlled":"1","volume":293,"extern":"1","page":"8379-8393","publication_identifier":{"issn":["0021-9258","1083-351X"]},"month":"06","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."}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"None","day":"01","publication_status":"published","author":[{"last_name":"Weinhäupl","full_name":"Weinhäupl, Katharina","first_name":"Katharina"},{"last_name":"Brennich","first_name":"Martha","full_name":"Brennich, Martha"},{"full_name":"Kazmaier, Uli","first_name":"Uli","last_name":"Kazmaier"},{"last_name":"Lelievre","full_name":"Lelievre, Joel","first_name":"Joel"},{"full_name":"Ballell, Lluis","first_name":"Lluis","last_name":"Ballell"},{"full_name":"Goldberg, Alfred","first_name":"Alfred","last_name":"Goldberg"},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul"},{"last_name":"Fraga","first_name":"Hugo","full_name":"Fraga, Hugo"}]},{"citation":{"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.","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>","short":"D. Samanta, D. Galaktionova, J. Gemen, L.J.W. Shimon, Y. Diskin-Posner, L. Avram, P. Král, R. Klajn, Nature Communications 9 (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.” <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>.","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>"},"date_created":"2023-08-01T09:39:32Z","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"year":"2018","related_material":{"link":[{"url":"https://doi.org/10.1038/s41467-018-03701-2","relation":"erratum"}]},"article_number":"641","_id":"13374","article_type":"original","doi":"10.1038/s41467-017-02715-6","publication_status":"published","external_id":{"pmid":["29440687"]},"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"}],"extern":"1","quality_controlled":"1","volume":9,"publisher":"Springer Nature","date_published":"2018-02-13T00:00:00Z","title":"Reversible chromism of spiropyran in the cavity of a flexible coordination cage","oa":1,"date_updated":"2023-08-07T10:54:05Z","article_processing_charge":"No","scopus_import":"1","intvolume":"         9","language":[{"iso":"eng"}],"publication":"Nature Communications","author":[{"first_name":"Dipak","full_name":"Samanta, Dipak","last_name":"Samanta"},{"full_name":"Galaktionova, Daria","first_name":"Daria","last_name":"Galaktionova"},{"full_name":"Gemen, Julius","first_name":"Julius","last_name":"Gemen"},{"first_name":"Linda J. W.","full_name":"Shimon, Linda J. W.","last_name":"Shimon"},{"last_name":"Diskin-Posner","full_name":"Diskin-Posner, Yael","first_name":"Yael"},{"first_name":"Liat","full_name":"Avram, Liat","last_name":"Avram"},{"last_name":"Král","first_name":"Petr","full_name":"Král, Petr"},{"last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","first_name":"Rafal","full_name":"Klajn, Rafal"}],"main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-02715-6","open_access":"1"}],"day":"13","oa_version":"Published Version","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","month":"02","publication_identifier":{"eissn":["2041-1723"]},"pmid":1,"status":"public","type":"journal_article"},{"publication":"Nature Communications","language":[{"iso":"eng"}],"intvolume":"         9","scopus_import":"1","date_updated":"2023-11-07T11:46:12Z","oa":1,"article_processing_charge":"No","title":"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB","pmid":1,"type":"journal_article","status":"public","month":"05","publication_identifier":{"issn":["2041-1723"]},"main_file_link":[{"url":"https://doi.org/10.1038/s41467-018-04139-2","open_access":"1"}],"oa_version":"Published Version","day":"04","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"first_name":"Bastian","full_name":"Bräuning, Bastian","last_name":"Bräuning"},{"last_name":"Bertosin","full_name":"Bertosin, Eva","first_name":"Eva"},{"full_name":"Praetorius, Florian M","first_name":"Florian M","id":"dfec9381-4341-11ee-8fd8-faa02bba7d62","last_name":"Praetorius"},{"first_name":"Christian","full_name":"Ihling, Christian","last_name":"Ihling"},{"full_name":"Schatt, Alexandra","first_name":"Alexandra","last_name":"Schatt"},{"last_name":"Adler","first_name":"Agnes","full_name":"Adler, Agnes"},{"last_name":"Richter","full_name":"Richter, Klaus","first_name":"Klaus"},{"last_name":"Sinz","full_name":"Sinz, Andrea","first_name":"Andrea"},{"last_name":"Dietz","first_name":"Hendrik","full_name":"Dietz, Hendrik"},{"first_name":"Michael","full_name":"Groll, Michael","last_name":"Groll"}],"doi":"10.1038/s41467-018-04139-2","article_type":"original","_id":"14284","article_number":"1806","year":"2018","date_created":"2023-09-06T12:07:33Z","citation":{"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.","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>","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).","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.” <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>.","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>"},"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"publisher":"Springer Nature","date_published":"2018-05-04T00:00:00Z","extern":"1","quality_controlled":"1","volume":9,"external_id":{"pmid":["29728606"]},"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"}],"publication_status":"published"},{"publication_identifier":{"issn":["2041-2649"],"eissn":["2041-2657"]},"month":"09","main_file_link":[{"url":"https://doi.org/10.1093/bfgp/ely007","open_access":"1"}],"oa_version":"Published Version","day":"01","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","author":[{"first_name":"Moriyama","full_name":"Yuuta, Moriyama","id":"4968E7C8-F248-11E8-B48F-1D18A9856A87","last_name":"Yuuta","orcid":"0000-0002-2853-8051"},{"full_name":"Koshiba-Takeuchi, Kazuko","first_name":"Kazuko","last_name":"Koshiba-Takeuchi"}],"pmid":1,"status":"public","type":"journal_article","isi":1,"intvolume":"        17","scopus_import":"1","date_updated":"2023-09-19T15:11:22Z","oa":1,"issue":"5","article_processing_charge":"No","title":"Significance of whole-genome duplications on the emergence of evolutionary novelties","publication":"Briefings in Functional Genomics","language":[{"iso":"eng"}],"external_id":{"pmid":["29579140"],"isi":["000456054400004"]},"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."}],"publication_status":"published","publisher":"Oxford University Press","date_published":"2018-09-01T00:00:00Z","page":"329-338","department":[{"_id":"CaHe"}],"quality_controlled":"1","volume":17,"acknowledgement":"This work was supported by JSPS overseas research fellowships (Y.M.) and SENSHIN Medical Research Foundation (K.K.T.).","year":"2018","date_created":"2022-03-18T12:40:35Z","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>","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.","short":"M. Yuuta, K. Koshiba-Takeuchi, Briefings in Functional Genomics 17 (2018) 329–338.","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>.","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.” <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>.","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>"},"keyword":["Genetics","Molecular Biology","Biochemistry","General Medicine"],"doi":"10.1093/bfgp/ely007","_id":"10880","article_type":"original"},{"author":[{"full_name":"Walt, Samuel G.","first_name":"Samuel G.","last_name":"Walt"},{"last_name":"Bhargava Ram","full_name":"Bhargava Ram, Niraghatam","first_name":"Niraghatam"},{"last_name":"Atala","full_name":"Atala, Marcos","first_name":"Marcos"},{"first_name":"Nikolay I","full_name":"Shvetsov-Shilovski, Nikolay I","last_name":"Shvetsov-Shilovski"},{"last_name":"von Conta","full_name":"von Conta, Aaron","first_name":"Aaron"},{"id":"71b4d059-2a03-11ee-914d-dfa3beed6530","last_name":"Baykusheva","full_name":"Baykusheva, Denitsa Rangelova","first_name":"Denitsa Rangelova"},{"last_name":"Lein","first_name":"Manfred","full_name":"Lein, Manfred"},{"first_name":"Hans Jakob","full_name":"Wörner, Hans Jakob","last_name":"Wörner"}],"month":"06","publication_identifier":{"eissn":["2041-1723"]},"day":"15","main_file_link":[{"url":"https://doi.org/10.1038/ncomms15651","open_access":"1"}],"oa_version":"Published Version","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","pmid":1,"status":"public","type":"journal_article","date_updated":"2023-08-22T08:26:06Z","oa":1,"article_processing_charge":"No","title":"Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering","intvolume":"         8","scopus_import":"1","language":[{"iso":"eng"}],"publication":"Nature Communications","publication_status":"published","external_id":{"pmid":["28643771"]},"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."}],"publisher":"Springer Nature","date_published":"2017-06-15T00:00:00Z","extern":"1","volume":8,"quality_controlled":"1","year":"2017","date_created":"2023-08-10T06:36:09Z","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>","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.","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).","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.” <i>Nature Communications</i>, vol. 8, 15651, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/ncomms15651\">10.1038/ncomms15651</a>.","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>."},"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"article_number":"15651","_id":"14005","article_type":"original","doi":"10.1038/ncomms15651"},{"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","file":[{"file_name":"2017_eLife_Helle.pdf","checksum":"c35f42dcfb007f6d6c761a27e24c26d3","file_id":"10372","success":1,"date_updated":"2021-11-29T09:07:41Z","date_created":"2021-11-29T09:07:41Z","creator":"cchlebak","access_level":"open_access","content_type":"application/pdf","relation":"main_file","file_size":6120157}],"oa_version":"Published Version","main_file_link":[{"url":"https://elifesciences.org/articles/30292","open_access":"1"}],"day":"09","publication_identifier":{"issn":["2050-084X"]},"month":"11","author":[{"first_name":"Sebastian Carsten Johannes","full_name":"Helle, Sebastian Carsten Johannes","last_name":"Helle"},{"full_name":"Feng, Qian","first_name":"Qian","last_name":"Feng"},{"full_name":"Aebersold, Mathias J","first_name":"Mathias J","last_name":"Aebersold"},{"first_name":"Luca","full_name":"Hirt, Luca","last_name":"Hirt"},{"last_name":"Grüter","first_name":"Raphael R","full_name":"Grüter, Raphael R"},{"first_name":"Afshin","full_name":"Vahid, Afshin","last_name":"Vahid"},{"last_name":"Sirianni","first_name":"Andrea","full_name":"Sirianni, Andrea"},{"last_name":"Mostowy","first_name":"Serge","full_name":"Mostowy, Serge"},{"first_name":"Jess G","full_name":"Snedeker, Jess G","last_name":"Snedeker"},{"first_name":"Anđela","full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139","last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b"},{"last_name":"Idema","first_name":"Timon","full_name":"Idema, Timon"},{"full_name":"Zambelli, Tomaso","first_name":"Tomaso","last_name":"Zambelli"},{"last_name":"Kornmann","full_name":"Kornmann, Benoît","first_name":"Benoît"}],"status":"public","type":"journal_article","pmid":1,"scopus_import":"1","has_accepted_license":"1","intvolume":"         6","title":"Mechanical force induces mitochondrial fission","article_processing_charge":"No","oa":1,"date_updated":"2021-11-29T09:28:14Z","publication":"eLife","language":[{"iso":"eng"}],"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."}],"external_id":{"pmid":["29119945"]},"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"ddc":["572"],"publication_status":"published","quality_controlled":"1","volume":6,"extern":"1","date_published":"2017-11-09T00:00:00Z","publisher":"eLife Sciences Publications","article_number":"e30292","keyword":["general immunology and microbiology","general biochemistry","genetics and molecular biology","general medicine","general neuroscience"],"date_created":"2021-11-29T08:51:38Z","citation":{"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>","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>.","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>.","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.","ieee":"S. C. J. Helle <i>et al.</i>, “Mechanical force induces mitochondrial fission,” <i>eLife</i>, vol. 6. eLife Sciences Publications, 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>","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)."},"year":"2017","doi":"10.7554/elife.30292","_id":"10370","article_type":"original","file_date_updated":"2021-11-29T09:07:41Z"},{"volume":8,"quality_controlled":"1","extern":"1","date_published":"2017-08-30T00:00:00Z","publisher":"Springer Nature","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."}],"external_id":{"pmid":["28855503"]},"publication_status":"published","doi":"10.1038/s41467-017-00322-z","article_type":"original","_id":"11065","article_number":"328","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"date_created":"2022-04-07T07:45:50Z","citation":{"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>","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>.","short":"A. Buchwalter, M. Hetzer, Nature Communications 8 (2017).","ieee":"A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","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>"},"year":"2017","type":"journal_article","status":"public","pmid":1,"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa_version":"Published Version","main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-00322-z","open_access":"1"}],"day":"30","month":"08","publication_identifier":{"issn":["2041-1723"]},"author":[{"full_name":"Buchwalter, Abigail","first_name":"Abigail","last_name":"Buchwalter"},{"first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"}],"publication":"Nature Communications","language":[{"iso":"eng"}],"scopus_import":"1","intvolume":"         8","title":"Nucleolar expansion and elevated protein translation in premature aging","article_processing_charge":"No","oa":1,"date_updated":"2022-07-18T08:33:03Z"},{"publication":"Nature Communications","language":[{"iso":"eng"}],"scopus_import":"1","intvolume":"         7","title":"p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis","oa":1,"date_updated":"2022-07-18T08:34:32Z","article_processing_charge":"No","pmid":1,"type":"journal_article","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms13874"}],"oa_version":"Published Version","day":"22","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","month":"12","publication_identifier":{"issn":["2041-1723"]},"author":[{"full_name":"van de Ven, Robert A.H.","first_name":"Robert A.H.","last_name":"van de Ven"},{"last_name":"de Groot","full_name":"de Groot, Jolien S.","first_name":"Jolien S."},{"last_name":"Park","full_name":"Park, Danielle","first_name":"Danielle"},{"last_name":"van Domselaar","full_name":"van Domselaar, Robert","first_name":"Robert"},{"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"},{"last_name":"Rueda","full_name":"Rueda, Oscar M.","first_name":"Oscar M."},{"last_name":"Ali","first_name":"H. Raza","full_name":"Ali, H. Raza"},{"full_name":"Caldas, Carlos","first_name":"Carlos","last_name":"Caldas"},{"last_name":"van Diest","first_name":"Paul J.","full_name":"van Diest, Paul J."},{"last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W"},{"last_name":"Sahai","first_name":"Erik","full_name":"Sahai, Erik"},{"first_name":"Patrick W.B.","full_name":"Derksen, Patrick W.B.","last_name":"Derksen"}],"doi":"10.1038/ncomms13874","_id":"11072","article_type":"original","article_number":"13874","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/ncomms16030"}]},"citation":{"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).","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>","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.","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>.","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.","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>.","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>"},"date_created":"2022-04-07T07:48:34Z","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"year":"2016","extern":"1","volume":7,"quality_controlled":"1","publisher":"Springer Nature","date_published":"2016-12-22T00:00:00Z","external_id":{"pmid":["28004812"]},"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"}],"publication_status":"published"},{"publication_identifier":{"issn":["2041-1723"]},"month":"10","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","abstract":[{"lang":"eng","text":"The large majority of three-dimensional structures of biological macromolecules have been determined by X-ray diffraction of crystalline samples. High-resolution structure determination crucially depends on the homogeneity of the protein crystal. Overall ‘rocking’ motion of molecules in the crystal is expected to influence diffraction quality, and such motion may therefore affect the process of solving crystal structures. Yet, so far overall molecular motion has not directly been observed in protein crystals, and the timescale of such dynamics remains unclear. Here we use solid-state NMR, X-ray diffraction methods and μs-long molecular dynamics simulations to directly characterize the rigid-body motion of a protein in different crystal forms. For ubiquitin crystals investigated in this study we determine the range of possible correlation times of rocking motion, 0.1–100 μs. The amplitude of rocking varies from one crystal form to another and is correlated with the resolution obtainable in X-ray diffraction experiments."}],"day":"05","oa_version":"Published Version","author":[{"first_name":"Peixiang","full_name":"Ma, Peixiang","last_name":"Ma"},{"last_name":"Xue","first_name":"Yi","full_name":"Xue, Yi"},{"last_name":"Coquelle","first_name":"Nicolas","full_name":"Coquelle, Nicolas"},{"last_name":"Haller","full_name":"Haller, Jens D.","first_name":"Jens D."},{"full_name":"Yuwen, Tairan","first_name":"Tairan","last_name":"Yuwen"},{"first_name":"Isabel","full_name":"Ayala, Isabel","last_name":"Ayala"},{"full_name":"Mikhailovskii, Oleg","first_name":"Oleg","last_name":"Mikhailovskii"},{"first_name":"Dieter","full_name":"Willbold, Dieter","last_name":"Willbold"},{"full_name":"Colletier, Jacques-Philippe","first_name":"Jacques-Philippe","last_name":"Colletier"},{"last_name":"Skrynnikov","first_name":"Nikolai R.","full_name":"Skrynnikov, Nikolai R."},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul"}],"publication_status":"published","status":"public","type":"journal_article","date_published":"2015-10-05T00:00:00Z","publisher":"Springer Nature","quality_controlled":"1","volume":6,"extern":"1","article_number":"8361","intvolume":"         6","year":"2015","article_processing_charge":"No","date_updated":"2021-01-12T08:19:24Z","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"title":"Observing the overall rocking motion of a protein in a crystal","date_created":"2020-09-18T10:07:36Z","citation":{"short":"P. Ma, Y. Xue, N. Coquelle, J.D. Haller, T. Yuwen, I. Ayala, O. Mikhailovskii, D. Willbold, J.-P. Colletier, N.R. Skrynnikov, P. Schanda, Nature Communications 6 (2015).","ieee":"P. Ma <i>et al.</i>, “Observing the overall rocking motion of a protein in a crystal,” <i>Nature Communications</i>, vol. 6. Springer Nature, 2015.","ama":"Ma P, Xue Y, Coquelle N, et al. Observing the overall rocking motion of a protein in a crystal. <i>Nature Communications</i>. 2015;6. doi:<a href=\"https://doi.org/10.1038/ncomms9361\">10.1038/ncomms9361</a>","ista":"Ma P, Xue Y, Coquelle N, Haller JD, Yuwen T, Ayala I, Mikhailovskii O, Willbold D, Colletier J-P, Skrynnikov NR, Schanda P. 2015. Observing the overall rocking motion of a protein in a crystal. Nature Communications. 6, 8361.","chicago":"Ma, Peixiang, Yi Xue, Nicolas Coquelle, Jens D. Haller, Tairan Yuwen, Isabel Ayala, Oleg Mikhailovskii, et al. “Observing the Overall Rocking Motion of a Protein in a Crystal.” <i>Nature Communications</i>. Springer Nature, 2015. <a href=\"https://doi.org/10.1038/ncomms9361\">https://doi.org/10.1038/ncomms9361</a>.","mla":"Ma, Peixiang, et al. “Observing the Overall Rocking Motion of a Protein in a Crystal.” <i>Nature Communications</i>, vol. 6, 8361, Springer Nature, 2015, doi:<a href=\"https://doi.org/10.1038/ncomms9361\">10.1038/ncomms9361</a>.","apa":"Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., … Schanda, P. (2015). Observing the overall rocking motion of a protein in a crystal. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms9361\">https://doi.org/10.1038/ncomms9361</a>"},"publication":"Nature Communications","doi":"10.1038/ncomms9361","language":[{"iso":"eng"}],"_id":"8456","article_type":"original"},{"scopus_import":"1","intvolume":"         6","article_processing_charge":"No","oa":1,"date_updated":"2023-08-22T08:52:56Z","title":"Observation of laser-induced electronic structure in oriented polyatomic molecules","publication":"Nature Communications","language":[{"iso":"eng"}],"month":"05","publication_identifier":{"eissn":["2041-1723"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"Published Version","day":"05","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms8039"}],"author":[{"first_name":"P. M.","full_name":"Kraus, P. M.","last_name":"Kraus"},{"full_name":"Tolstikhin, O. I.","first_name":"O. I.","last_name":"Tolstikhin"},{"id":"71b4d059-2a03-11ee-914d-dfa3beed6530","last_name":"Baykusheva","full_name":"Baykusheva, Denitsa Rangelova","first_name":"Denitsa Rangelova"},{"full_name":"Rupenyan, A.","first_name":"A.","last_name":"Rupenyan"},{"full_name":"Schneider, J.","first_name":"J.","last_name":"Schneider"},{"full_name":"Bisgaard, C. Z.","first_name":"C. Z.","last_name":"Bisgaard"},{"first_name":"T.","full_name":"Morishita, T.","last_name":"Morishita"},{"full_name":"Jensen, F.","first_name":"F.","last_name":"Jensen"},{"last_name":"Madsen","full_name":"Madsen, L. B.","first_name":"L. B."},{"last_name":"Wörner","full_name":"Wörner, H. J.","first_name":"H. J."}],"type":"journal_article","status":"public","pmid":1,"article_number":"7039","year":"2015","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"citation":{"apa":"Kraus, P. M., Tolstikhin, O. I., Baykusheva, D. R., Rupenyan, A., Schneider, J., Bisgaard, C. Z., … Wörner, H. J. (2015). Observation of laser-induced electronic structure in oriented polyatomic molecules. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms8039\">https://doi.org/10.1038/ncomms8039</a>","chicago":"Kraus, P. M., O. I. Tolstikhin, Denitsa Rangelova Baykusheva, A. Rupenyan, J. Schneider, C. Z. Bisgaard, T. Morishita, F. Jensen, L. B. Madsen, and H. J. Wörner. “Observation of Laser-Induced Electronic Structure in Oriented Polyatomic Molecules.” <i>Nature Communications</i>. Springer Nature, 2015. <a href=\"https://doi.org/10.1038/ncomms8039\">https://doi.org/10.1038/ncomms8039</a>.","ista":"Kraus PM, Tolstikhin OI, Baykusheva DR, Rupenyan A, Schneider J, Bisgaard CZ, Morishita T, Jensen F, Madsen LB, Wörner HJ. 2015. Observation of laser-induced electronic structure in oriented polyatomic molecules. Nature Communications. 6, 7039.","mla":"Kraus, P. M., et al. “Observation of Laser-Induced Electronic Structure in Oriented Polyatomic Molecules.” <i>Nature Communications</i>, vol. 6, 7039, Springer Nature, 2015, doi:<a href=\"https://doi.org/10.1038/ncomms8039\">10.1038/ncomms8039</a>.","short":"P.M. Kraus, O.I. Tolstikhin, D.R. Baykusheva, A. Rupenyan, J. Schneider, C.Z. Bisgaard, T. Morishita, F. Jensen, L.B. Madsen, H.J. Wörner, Nature Communications 6 (2015).","ieee":"P. M. Kraus <i>et al.</i>, “Observation of laser-induced electronic structure in oriented polyatomic molecules,” <i>Nature Communications</i>, vol. 6. Springer Nature, 2015.","ama":"Kraus PM, Tolstikhin OI, Baykusheva DR, et al. Observation of laser-induced electronic structure in oriented polyatomic molecules. <i>Nature Communications</i>. 2015;6. doi:<a href=\"https://doi.org/10.1038/ncomms8039\">10.1038/ncomms8039</a>"},"date_created":"2023-08-10T06:38:01Z","doi":"10.1038/ncomms8039","_id":"14016","article_type":"original","abstract":[{"text":"All attosecond time-resolved measurements have so far relied on the use of intense near-infrared laser pulses. In particular, attosecond streaking, laser-induced electron diffraction and high-harmonic generation all make use of non-perturbative light–matter interactions. Remarkably, the effect of the strong laser field on the studied sample has often been neglected in previous studies. Here we use high-harmonic spectroscopy to measure laser-induced modifications of the electronic structure of molecules. We study high-harmonic spectra of spatially oriented CH3F and CH3Br as generic examples of polar polyatomic molecules. We accurately measure intensity ratios of even and odd-harmonic orders, and of the emission from aligned and unaligned molecules. We show that these robust observables reveal a substantial modification of the molecular electronic structure by the external laser field. Our insights offer new challenges and opportunities for a range of emerging strong-field attosecond spectroscopies.","lang":"eng"}],"external_id":{"pmid":["25940229"]},"publication_status":"published","date_published":"2015-05-05T00:00:00Z","publisher":"Springer Nature","volume":6,"quality_controlled":"1","extern":"1"}]