[{"quality_controlled":"1","doi":"10.7554/elife.49796","publication_identifier":{"issn":["2050-084X"]},"language":[{"iso":"eng"}],"keyword":["General Immunology and Microbiology","General Biochemistry","Genetics and Molecular Biology","General Medicine","General Neuroscience"],"article_number":"e49796","title":"Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress","day":"10","file":[{"file_size":6984654,"relation":"main_file","content_type":"application/pdf","creator":"dernst","file_name":"2019_eLife_Buchwalter.pdf","success":1,"date_created":"2022-04-08T08:18:01Z","access_level":"open_access","file_id":"11138","date_updated":"2022-04-08T08:18:01Z","checksum":"1e8672a1e9c3dc0a2d3d0dad89673616"}],"author":[{"full_name":"Buchwalter, Abigail","first_name":"Abigail","last_name":"Buchwalter"},{"first_name":"Roberta","last_name":"Schulte","full_name":"Schulte, Roberta"},{"full_name":"Tsai, Hsiao","first_name":"Hsiao","last_name":"Tsai"},{"full_name":"Capitanio, Juliana","last_name":"Capitanio","first_name":"Juliana"},{"orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"article_type":"original","article_processing_charge":"No","scopus_import":"1","publication":"eLife","pmid":1,"publisher":"eLife Sciences Publications","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","ddc":["570"],"date_published":"2019-10-10T00:00:00Z","has_accepted_license":"1","oa":1,"publication_status":"published","citation":{"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>","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.","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>.","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>","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.","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>.","short":"A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, M. Hetzer, ELife 8 (2019)."},"extern":"1","related_material":{"record":[{"id":"13079","status":"public","relation":"research_data"}]},"intvolume":"         8","external_id":{"pmid":["31599721"]},"status":"public","file_date_updated":"2022-04-08T08:18:01Z","date_created":"2022-04-07T07:45:02Z","volume":8,"oa_version":"Published Version","type":"journal_article","month":"10","abstract":[{"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.","lang":"eng"}],"date_updated":"2023-05-31T06:36:22Z","_id":"11060","year":"2019"},{"title":"Age mosaicism across multiple scales in adult tissues","day":"06","author":[{"full_name":"Arrojo e Drigo, Rafael","last_name":"Arrojo e Drigo","first_name":"Rafael"},{"full_name":"Lev-Ram, Varda","first_name":"Varda","last_name":"Lev-Ram"},{"full_name":"Tyagi, Swati","last_name":"Tyagi","first_name":"Swati"},{"full_name":"Ramachandra, Ranjan","last_name":"Ramachandra","first_name":"Ranjan"},{"last_name":"Deerinck","first_name":"Thomas","full_name":"Deerinck, Thomas"},{"last_name":"Bushong","first_name":"Eric","full_name":"Bushong, Eric"},{"last_name":"Phan","first_name":"Sebastien","full_name":"Phan, Sebastien"},{"full_name":"Orphan, Victoria","first_name":"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"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"article_processing_charge":"No","scopus_import":"1","article_type":"original","publication":"Cell Metabolism","pmid":1,"publisher":"Elsevier","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","quality_controlled":"1","doi":"10.1016/j.cmet.2019.05.010","publication_identifier":{"issn":["1550-4131"]},"language":[{"iso":"eng"}],"issue":"2","keyword":["Cell Biology","Molecular Biology","Physiology"],"date_created":"2022-04-07T07:45:21Z","volume":30,"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."}],"date_updated":"2022-07-18T08:32:30Z","oa_version":"Published Version","type":"journal_article","month":"08","page":"343-351.e3","_id":"11062","year":"2019","main_file_link":[{"url":"https://doi.org/10.1016/j.cmet.2019.05.010","open_access":"1"}],"date_published":"2019-08-06T00:00:00Z","oa":1,"publication_status":"published","citation":{"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.","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>.","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.","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>","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>.","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.","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>"},"extern":"1","intvolume":"        30","status":"public","external_id":{"pmid":["31178361"]}},{"year":"2019","_id":"8405","oa_version":"Published Version","month":"06","type":"journal_article","date_updated":"2021-01-12T08:19:03Z","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"}],"volume":10,"date_created":"2020-09-17T10:28:25Z","external_id":{"pmid":["31217444"]},"status":"public","extern":"1","intvolume":"        10","citation":{"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).","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>.","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.","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>","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.","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>.","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>"},"oa":1,"publication_status":"published","date_published":"2019-06-19T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1038/s41467-019-10490-9","open_access":"1"}],"publisher":"Springer Nature","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","pmid":1,"publication":"Nature Communications","article_type":"original","article_processing_charge":"No","author":[{"last_name":"Gauto","first_name":"Diego F.","full_name":"Gauto, Diego F."},{"last_name":"Estrozi","first_name":"Leandro F.","full_name":"Estrozi, Leandro F."},{"last_name":"Schwieters","first_name":"Charles D.","full_name":"Schwieters, Charles D."},{"full_name":"Effantin, Gregory","last_name":"Effantin","first_name":"Gregory"},{"first_name":"Pavel","last_name":"Macek","full_name":"Macek, Pavel"},{"full_name":"Sounier, Remy","first_name":"Remy","last_name":"Sounier"},{"first_name":"Astrid C.","last_name":"Sivertsen","full_name":"Sivertsen, Astrid C."},{"full_name":"Schmidt, Elena","last_name":"Schmidt","first_name":"Elena"},{"full_name":"Kerfah, Rime","first_name":"Rime","last_name":"Kerfah"},{"first_name":"Guillaume","last_name":"Mas","full_name":"Mas, Guillaume"},{"full_name":"Colletier, Jacques-Philippe","last_name":"Colletier","first_name":"Jacques-Philippe"},{"full_name":"Güntert, Peter","first_name":"Peter","last_name":"Güntert"},{"last_name":"Favier","first_name":"Adrien","full_name":"Favier, Adrien"},{"full_name":"Schoehn, Guy","last_name":"Schoehn","first_name":"Guy"},{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda"},{"last_name":"Boisbouvier","first_name":"Jerome","full_name":"Boisbouvier, Jerome"}],"day":"19","article_number":"2697","title":"Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["2041-1723"]},"doi":"10.1038/s41467-019-10490-9","quality_controlled":"1"},{"external_id":{"pmid":["31543461"]},"status":"public","intvolume":"        26","extern":"1","citation":{"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.","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>.","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.","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>","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.","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>.","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>"},"oa":1,"publication_status":"published","date_published":"2019-11-21T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1016/j.chembiol.2019.09.002","open_access":"1"}],"year":"2019","_id":"9018","page":"1573-1585.e10","oa_version":"Published Version","month":"11","type":"journal_article","date_updated":"2023-02-23T13:46:53Z","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"}],"volume":26,"date_created":"2021-01-19T11:04:50Z","keyword":["Clinical Biochemistry","Molecular Medicine","Biochemistry","Molecular Biology","Pharmacology","Drug Discovery"],"issue":"11","language":[{"iso":"eng"}],"publication_identifier":{"issn":["2451-9456"]},"doi":"10.1016/j.chembiol.2019.09.002","quality_controlled":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Elsevier","pmid":1,"publication":"Cell Chemical Biology","article_type":"original","article_processing_charge":"No","author":[{"full_name":"Bakail, May M","id":"FB3C3F8E-522F-11EA-B186-22963DDC885E","orcid":"0000-0002-9592-1587","first_name":"May M","last_name":"Bakail"},{"full_name":"Gaubert, Albane","first_name":"Albane","last_name":"Gaubert"},{"full_name":"Andreani, Jessica","last_name":"Andreani","first_name":"Jessica"},{"first_name":"Gwenaëlle","last_name":"Moal","full_name":"Moal, Gwenaëlle"},{"full_name":"Pinna, Guillaume","first_name":"Guillaume","last_name":"Pinna"},{"full_name":"Boyarchuk, Ekaterina","last_name":"Boyarchuk","first_name":"Ekaterina"},{"last_name":"Gaillard","first_name":"Marie-Cécile","full_name":"Gaillard, Marie-Cécile"},{"full_name":"Courbeyrette, Regis","first_name":"Regis","last_name":"Courbeyrette"},{"first_name":"Carl","last_name":"Mann","full_name":"Mann, Carl"},{"first_name":"Jean-Yves","last_name":"Thuret","full_name":"Thuret, Jean-Yves"},{"full_name":"Guichard, Bérengère","last_name":"Guichard","first_name":"Bérengère"},{"full_name":"Murciano, Brice","last_name":"Murciano","first_name":"Brice"},{"last_name":"Richet","first_name":"Nicolas","full_name":"Richet, Nicolas"},{"last_name":"Poitou","first_name":"Adeline","full_name":"Poitou, Adeline"},{"first_name":"Claire","last_name":"Frederic","full_name":"Frederic, Claire"},{"full_name":"Le Du, Marie-Hélène","first_name":"Marie-Hélène","last_name":"Le Du"},{"full_name":"Agez, Morgane","first_name":"Morgane","last_name":"Agez"},{"full_name":"Roelants, Caroline","last_name":"Roelants","first_name":"Caroline"},{"first_name":"Zachary A.","last_name":"Gurard-Levin","full_name":"Gurard-Levin, Zachary A."},{"full_name":"Almouzni, Geneviève","last_name":"Almouzni","first_name":"Geneviève"},{"first_name":"Nadia","last_name":"Cherradi","full_name":"Cherradi, Nadia"},{"first_name":"Raphael","last_name":"Guerois","full_name":"Guerois, Raphael"},{"last_name":"Ochsenbein","first_name":"Françoise","full_name":"Ochsenbein, Françoise"}],"day":"21","title":"Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1"},{"extern":"1","intvolume":"        10","citation":{"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>","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>","ista":"Ramananarivo S, Ducrot E, Palacci JA. 2019. Activity-controlled annealing of colloidal monolayers. Nature Communications. 10(1), 3380.","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>.","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>.","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.","short":"S. Ramananarivo, E. Ducrot, J.A. Palacci, Nature Communications 10 (2019)."},"status":"public","external_id":{"arxiv":["1909.07382"],"pmid":["31358762"]},"ddc":["530"],"date_published":"2019-07-29T00:00:00Z","publication_status":"published","oa":1,"has_accepted_license":"1","_id":"9060","year":"2019","volume":10,"date_created":"2021-02-02T13:43:36Z","file_date_updated":"2021-02-02T13:47:21Z","date_updated":"2023-02-23T13:47:59Z","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."}],"type":"journal_article","oa_version":"Published Version","month":"07","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"language":[{"iso":"eng"}],"issue":"1","doi":"10.1038/s41467-019-11362-y","quality_controlled":"1","publication_identifier":{"issn":["2041-1723"]},"publication":"Nature Communications","article_processing_charge":"No","scopus_import":"1","article_type":"original","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"publisher":"Springer Nature","user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","pmid":1,"arxiv":1,"title":"Activity-controlled annealing of colloidal monolayers","article_number":"3380","author":[{"full_name":"Ramananarivo, Sophie","first_name":"Sophie","last_name":"Ramananarivo"},{"first_name":"Etienne","last_name":"Ducrot","full_name":"Ducrot, Etienne"},{"full_name":"Palacci, Jérémie A","id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d","orcid":"0000-0002-7253-9465","last_name":"Palacci","first_name":"Jérémie A"}],"day":"29","file":[{"success":1,"file_name":"2019_NatureComm_Ramananarivo.pdf","relation":"main_file","content_type":"application/pdf","file_size":2820337,"creator":"cziletti","date_updated":"2021-02-02T13:47:21Z","file_id":"9061","checksum":"70c6e5d6fbea0932b0669505ab6633ec","date_created":"2021-02-02T13:47:21Z","access_level":"open_access"}]},{"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.","year":"2019","_id":"10355","page":"43-52","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"}],"date_updated":"2021-11-26T11:54:25Z","oa_version":"Preprint","type":"journal_article","month":"06","volume":58,"date_created":"2021-11-26T11:33:21Z","external_id":{"pmid":["31226513"]},"status":"public","extern":"1","intvolume":"        58","citation":{"short":"A.E. Hafner, J. Krausser, A. Šarić, Current Opinion in Structural Biology 58 (2019) 43–52.","chicago":"Hafner, Anne E, Johannes Krausser, and Anđela Šarić. “Minimal Coarse-Grained Models for Molecular Self-Organisation in Biology.” <i>Current Opinion in Structural Biology</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.sbi.2019.05.018\">https://doi.org/10.1016/j.sbi.2019.05.018</a>.","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.","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>","ista":"Hafner AE, Krausser J, Šarić A. 2019. Minimal coarse-grained models for molecular self-organisation in biology. Current Opinion in Structural Biology. 58, 43–52.","mla":"Hafner, Anne E., et al. “Minimal Coarse-Grained Models for Molecular Self-Organisation in Biology.” <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>.","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>"},"publication_status":"published","oa":1,"date_published":"2019-06-18T00:00:00Z","main_file_link":[{"url":"https://arxiv.org/abs/1906.09349","open_access":"1"}],"publisher":"Elsevier","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","pmid":1,"publication":"Current Opinion in Structural Biology","scopus_import":"1","article_processing_charge":"No","article_type":"original","author":[{"first_name":"Anne E","last_name":"Hafner","full_name":"Hafner, Anne E"},{"last_name":"Krausser","first_name":"Johannes","full_name":"Krausser, Johannes"},{"first_name":"Anđela","last_name":"Šarić","full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139","id":"bf63d406-f056-11eb-b41d-f263a6566d8b"}],"day":"18","title":"Minimal coarse-grained models for molecular self-organisation in biology","keyword":["molecular biology","structural biology"],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["0959-440X"]},"doi":"10.1016/j.sbi.2019.05.018","quality_controlled":"1"},{"volume":29,"date_created":"2023-01-16T09:16:33Z","page":"2676-2686.e3","date_updated":"2023-05-08T10:54:54Z","abstract":[{"text":"Meiotic crossover frequency varies within genomes, which influences genetic diversity and adaptation. In turn, genetic variation within populations can act to modify crossover frequency in cis and trans. To identify genetic variation that controls meiotic crossover frequency, we screened Arabidopsis accessions using fluorescent recombination reporters. We mapped a genetic modifier of crossover frequency in Col × Bur populations of Arabidopsis to a premature stop codon within TBP-ASSOCIATED FACTOR 4b (TAF4b), which encodes a subunit of the RNA polymerase II general transcription factor TFIID. The Arabidopsis taf4b mutation is a rare variant found in the British Isles, originating in South-West Ireland. Using genetics, genomics, and immunocytology, we demonstrate a genome-wide decrease in taf4b crossovers, with strongest reduction in the sub-telomeric regions. Using RNA sequencing (RNA-seq) from purified meiocytes, we show that TAF4b expression is meiocyte enriched, whereas its paralog TAF4 is broadly expressed. Consistent with the role of TFIID in promoting gene expression, RNA-seq of wild-type and taf4b meiocytes identified widespread transcriptional changes, including in genes that regulate the meiotic cell cycle and recombination. Therefore, TAF4b duplication is associated with acquisition of meiocyte-specific expression and promotion of germline transcription, which act directly or indirectly to elevate crossovers. This identifies a novel mode of meiotic recombination control via a general transcription factor.","lang":"eng"}],"type":"journal_article","oa_version":"None","month":"08","_id":"12190","acknowledgement":"We thank Gregory Copenhaver (University of North Carolina), Avraham Levy (The Weizmann Institute), and Scott Poethig (University of Pennsylvania) for FTLs; Piotr Ziolkowski for Col-420/Bur seed; Sureshkumar Balasubramanian\r\n(Monash University) for providing British and Irish Arabidopsis accessions; Mathilde Grelon (INRA, Versailles) for providing the MLH1 antibody; and the Gurdon Institute for access to microscopes. This work was supported by a BBSRC DTP studentship (E.J.L.), European Research Area Network for Coordinating Action in Plant Sciences/BBSRC ‘‘DeCOP’’ (BB/M004937/1; C.L.), a BBSRC David Phillips Fellowship (BB/L025043/1; H.G. and X.F.), the European Research Council (CoG ‘‘SynthHotspot,’’ A.J.T., C.L., and I.R.H.; StG ‘‘SexMeth,’’ X.F.), and a Sainsbury Charitable Foundation Studentship (A.R.B.).","year":"2019","date_published":"2019-08-19T00:00:00Z","publication_status":"published","extern":"1","intvolume":"        29","citation":{"short":"E.J. Lawrence, H. Gao, A.J. Tock, C. Lambing, A.R. Blackwell, X. Feng, I.R. Henderson, Current Biology 29 (2019) 2676–2686.e3.","chicago":"Lawrence, Emma J., Hongbo Gao, Andrew J. Tock, Christophe Lambing, Alexander R. Blackwell, Xiaoqi Feng, and Ian R. Henderson. “Natural Variation in TBP-ASSOCIATED FACTOR 4b Controls Meiotic Crossover and Germline Transcription in Arabidopsis.” <i>Current Biology</i>. Elsevier BV, 2019. <a href=\"https://doi.org/10.1016/j.cub.2019.06.084\">https://doi.org/10.1016/j.cub.2019.06.084</a>.","ieee":"E. J. Lawrence <i>et al.</i>, “Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis,” <i>Current Biology</i>, vol. 29, no. 16. Elsevier BV, p. 2676–2686.e3, 2019.","apa":"Lawrence, E. J., Gao, H., Tock, A. J., Lambing, C., Blackwell, A. R., Feng, X., &#38; Henderson, I. R. (2019). Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis. <i>Current Biology</i>. Elsevier BV. <a href=\"https://doi.org/10.1016/j.cub.2019.06.084\">https://doi.org/10.1016/j.cub.2019.06.084</a>","mla":"Lawrence, Emma J., et al. “Natural Variation in TBP-ASSOCIATED FACTOR 4b Controls Meiotic Crossover and Germline Transcription in Arabidopsis.” <i>Current Biology</i>, vol. 29, no. 16, Elsevier BV, 2019, p. 2676–2686.e3, doi:<a href=\"https://doi.org/10.1016/j.cub.2019.06.084\">10.1016/j.cub.2019.06.084</a>.","ista":"Lawrence EJ, Gao H, Tock AJ, Lambing C, Blackwell AR, Feng X, Henderson IR. 2019. Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis. Current Biology. 29(16), 2676–2686.e3.","ama":"Lawrence EJ, Gao H, Tock AJ, et al. Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis. <i>Current Biology</i>. 2019;29(16):2676-2686.e3. doi:<a href=\"https://doi.org/10.1016/j.cub.2019.06.084\">10.1016/j.cub.2019.06.084</a>"},"external_id":{"pmid":["31378616"]},"status":"public","title":"Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis","author":[{"first_name":"Emma J.","last_name":"Lawrence","full_name":"Lawrence, Emma J."},{"last_name":"Gao","first_name":"Hongbo","full_name":"Gao, Hongbo"},{"full_name":"Tock, Andrew J.","first_name":"Andrew J.","last_name":"Tock"},{"first_name":"Christophe","last_name":"Lambing","full_name":"Lambing, Christophe"},{"last_name":"Blackwell","first_name":"Alexander R.","full_name":"Blackwell, Alexander R."},{"full_name":"Feng, Xiaoqi","id":"e0164712-22ee-11ed-b12a-d80fcdf35958","orcid":"0000-0002-4008-1234","first_name":"Xiaoqi","last_name":"Feng"},{"last_name":"Henderson","first_name":"Ian R.","full_name":"Henderson, Ian R."}],"day":"19","publication":"Current Biology","scopus_import":"1","article_processing_charge":"No","article_type":"original","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Elsevier BV","pmid":1,"department":[{"_id":"XiFe"}],"doi":"10.1016/j.cub.2019.06.084","quality_controlled":"1","publication_identifier":{"issn":["0960-9822"]},"keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"issue":"16"},{"file_date_updated":"2023-02-07T09:42:46Z","date_created":"2023-01-16T09:17:21Z","volume":8,"oa_version":"Published Version","month":"05","type":"journal_article","date_updated":"2023-05-08T10:54:12Z","abstract":[{"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.","lang":"eng"}],"_id":"12192","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).","main_file_link":[{"open_access":"1","url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6594752/"}],"date_published":"2019-05-28T00:00:00Z","ddc":["580"],"has_accepted_license":"1","publication_status":"published","oa":1,"citation":{"short":"S. He, M. Vickers, J. Zhang, X. Feng, ELife 8 (2019).","chicago":"He, Shengbo, Martin Vickers, Jingyi Zhang, and Xiaoqi Feng. “Natural Depletion of Histone H1 in Sex Cells Causes DNA Demethylation, Heterochromatin Decondensation and Transposon Activation.” <i>ELife</i>. eLife Sciences Publications, Ltd, 2019. <a href=\"https://doi.org/10.7554/elife.42530\">https://doi.org/10.7554/elife.42530</a>.","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.","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>","ista":"He S, Vickers M, Zhang J, Feng X. 2019. Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation. eLife. 8, 42530.","mla":"He, Shengbo, et al. “Natural Depletion of Histone H1 in Sex Cells Causes DNA Demethylation, Heterochromatin Decondensation and Transposon Activation.” <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>.","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>"},"intvolume":"         8","extern":"1","status":"public","external_id":{"unknown":["31135340"]},"article_number":"42530","title":"Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation","day":"28","file":[{"file_size":2493837,"relation":"main_file","content_type":"application/pdf","creator":"alisjak","file_name":"2019_elife_He.pdf","success":1,"date_created":"2023-02-07T09:42:46Z","access_level":"open_access","file_id":"12525","date_updated":"2023-02-07T09:42:46Z","checksum":"ea6b89c20d59e5eb3646916fe5d568ad"}],"author":[{"full_name":"He, Shengbo","last_name":"He","first_name":"Shengbo"},{"full_name":"Vickers, Martin","last_name":"Vickers","first_name":"Martin"},{"first_name":"Jingyi","last_name":"Zhang","full_name":"Zhang, Jingyi"},{"first_name":"Xiaoqi","last_name":"Feng","full_name":"Feng, Xiaoqi","id":"e0164712-22ee-11ed-b12a-d80fcdf35958","orcid":"0000-0002-4008-1234"}],"article_type":"original","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"scopus_import":"1","article_processing_charge":"No","publication":"eLife","department":[{"_id":"XiFe"}],"publisher":"eLife Sciences Publications, Ltd","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","quality_controlled":"1","doi":"10.7554/elife.42530","publication_identifier":{"issn":["2050-084X"]},"language":[{"iso":"eng"}],"keyword":["General Immunology and Microbiology","General Biochemistry","Genetics and Molecular Biology","General Medicine","General Neuroscience"]},{"language":[{"iso":"eng"}],"issue":"5","isi":1,"keyword":["Genetics","Molecular Biology","Biochemistry","General Medicine"],"quality_controlled":"1","doi":"10.1093/bfgp/ely007","publication_identifier":{"eissn":["2041-2657"],"issn":["2041-2649"]},"scopus_import":"1","article_processing_charge":"No","article_type":"original","publication":"Briefings in Functional Genomics","pmid":1,"department":[{"_id":"CaHe"}],"publisher":"Oxford University Press","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","title":"Significance of whole-genome duplications on the emergence of evolutionary novelties","day":"01","author":[{"last_name":"Yuuta","first_name":"Moriyama","id":"4968E7C8-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-2853-8051","full_name":"Yuuta, Moriyama"},{"full_name":"Koshiba-Takeuchi, Kazuko","last_name":"Koshiba-Takeuchi","first_name":"Kazuko"}],"citation":{"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.","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>.","short":"M. Yuuta, K. Koshiba-Takeuchi, Briefings in Functional Genomics 17 (2018) 329–338.","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>","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>"},"intvolume":"        17","external_id":{"isi":["000456054400004"],"pmid":["29579140"]},"status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1093/bfgp/ely007"}],"date_published":"2018-09-01T00:00:00Z","oa":1,"publication_status":"published","_id":"10880","year":"2018","acknowledgement":"This work was supported by JSPS overseas research fellowships (Y.M.) and SENSHIN Medical Research Foundation (K.K.T.).","date_created":"2022-03-18T12:40:35Z","volume":17,"abstract":[{"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.","lang":"eng"}],"date_updated":"2023-09-19T15:11:22Z","month":"09","oa_version":"Published Version","type":"journal_article","page":"329-338"},{"publication_identifier":{"issn":["0092-8674"]},"publication_status":"published","quality_controlled":"1","doi":"10.1016/j.cell.2018.10.039","date_published":"2018-11-15T00:00:00Z","status":"public","issue":"5","language":[{"iso":"eng"}],"citation":{"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>.","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.","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>","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.","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>.","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."},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"intvolume":"       175","extern":"1","month":"11","type":"journal_article","oa_version":"None","day":"15","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."}],"date_updated":"2021-01-12T08:19:15Z","page":"1365-1379.e25","author":[{"last_name":"Weinhäupl","first_name":"Katharina","full_name":"Weinhäupl, Katharina"},{"full_name":"Lindau, Caroline","last_name":"Lindau","first_name":"Caroline"},{"full_name":"Hessel, Audrey","last_name":"Hessel","first_name":"Audrey"},{"full_name":"Wang, Yong","last_name":"Wang","first_name":"Yong"},{"last_name":"Schütze","first_name":"Conny","full_name":"Schütze, Conny"},{"first_name":"Tobias","last_name":"Jores","full_name":"Jores, Tobias"},{"full_name":"Melchionda, Laura","first_name":"Laura","last_name":"Melchionda"},{"first_name":"Birgit","last_name":"Schönfisch","full_name":"Schönfisch, Birgit"},{"full_name":"Kalbacher, Hubert","first_name":"Hubert","last_name":"Kalbacher"},{"full_name":"Bersch, Beate","first_name":"Beate","last_name":"Bersch"},{"last_name":"Rapaport","first_name":"Doron","full_name":"Rapaport, Doron"},{"last_name":"Brennich","first_name":"Martha","full_name":"Brennich, Martha"},{"first_name":"Kresten","last_name":"Lindorff-Larsen","full_name":"Lindorff-Larsen, Kresten"},{"full_name":"Wiedemann, Nils","first_name":"Nils","last_name":"Wiedemann"},{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda"}],"date_created":"2020-09-18T10:04:39Z","volume":175,"title":"Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space","year":"2018","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Elsevier","article_type":"original","article_processing_charge":"No","_id":"8436","publication":"Cell"},{"author":[{"first_name":"Vilius","last_name":"Kurauskas","full_name":"Kurauskas, Vilius"},{"full_name":"Hessel, Audrey","last_name":"Hessel","first_name":"Audrey"},{"first_name":"François","last_name":"Dehez","full_name":"Dehez, François"},{"full_name":"Chipot, Christophe","first_name":"Christophe","last_name":"Chipot"},{"last_name":"Bersch","first_name":"Beate","full_name":"Bersch, Beate"},{"first_name":"Paul","last_name":"Schanda","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"}],"page":"745-747","date_updated":"2021-01-12T08:19:16Z","day":"03","month":"09","type":"journal_article","oa_version":"None","title":"Dynamics and interactions of AAC3 in DPC are not functionally relevant","volume":25,"date_created":"2020-09-18T10:04:59Z","publisher":"Springer Nature","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2018","publication":"Nature Structural & Molecular Biology","_id":"8438","article_processing_charge":"No","article_type":"letter_note","publication_status":"published","publication_identifier":{"issn":["1545-9993","1545-9985"]},"doi":"10.1038/s41594-018-0127-4","date_published":"2018-09-03T00:00:00Z","quality_controlled":"1","status":"public","extern":"1","intvolume":"        25","keyword":["Molecular Biology","Structural Biology"],"citation":{"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>.","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.","apa":"Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., &#38; Schanda, P. (2018). Dynamics and interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-018-0127-4\">https://doi.org/10.1038/s41594-018-0127-4</a>","ama":"Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. Dynamics and interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural &#38; Molecular Biology</i>. 2018;25(9):745-747. doi:<a href=\"https://doi.org/10.1038/s41594-018-0127-4\">10.1038/s41594-018-0127-4</a>","short":"V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature Structural &#38; Molecular Biology 25 (2018) 745–747.","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.","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>."},"language":[{"iso":"eng"}],"issue":"9"},{"quality_controlled":"1","date_published":"2018-06-01T00:00:00Z","doi":"10.1074/jbc.ra118.002251","publication_status":"published","publication_identifier":{"issn":["0021-9258","1083-351X"]},"language":[{"iso":"eng"}],"citation":{"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.","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>.","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.","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>","ista":"Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda P, Fraga H. 2018. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. 293(22), 8379–8393.","mla":"Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” <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>.","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>"},"issue":"22","extern":"1","intvolume":"       293","keyword":["Cell Biology","Biochemistry","Molecular Biology"],"status":"public","date_created":"2020-09-18T10:05:18Z","title":"The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis","volume":293,"date_updated":"2021-01-12T08:19:17Z","day":"01","abstract":[{"text":"Mycobacterium tuberculosis can remain dormant in the host, an ability that explains the failure of many current tuberculosis treatments. Recently, the natural products cyclomarin, ecumicin, and lassomycin have been shown to efficiently kill Mycobacterium tuberculosis persisters. Their target is the N-terminal domain of the hexameric AAA+ ATPase ClpC1, which recognizes, unfolds, and translocates protein substrates, such as proteins containing phosphorylated arginine residues, to the ClpP1P2 protease for degradation. Surprisingly, these antibiotics do not inhibit ClpC1 ATPase activity, and how they cause cell death is still unclear. Here, using NMR and small-angle X-ray scattering, we demonstrate that arginine-phosphate binding to the ClpC1 N-terminal domain induces millisecond dynamics. We show that these dynamics are caused by conformational changes and do not result from unfolding or oligomerization of this domain. Cyclomarin binding to this domain specifically blocked these N-terminal dynamics. On the basis of these results, we propose a mechanism of action involving cyclomarin-induced restriction of ClpC1 dynamics, which modulates the chaperone enzymatic activity leading eventually to cell death.","lang":"eng"}],"month":"06","oa_version":"None","type":"journal_article","page":"8379-8393","author":[{"full_name":"Weinhäupl, Katharina","last_name":"Weinhäupl","first_name":"Katharina"},{"full_name":"Brennich, Martha","last_name":"Brennich","first_name":"Martha"},{"last_name":"Kazmaier","first_name":"Uli","full_name":"Kazmaier, Uli"},{"full_name":"Lelievre, Joel","last_name":"Lelievre","first_name":"Joel"},{"first_name":"Lluis","last_name":"Ballell","full_name":"Ballell, Lluis"},{"last_name":"Goldberg","first_name":"Alfred","full_name":"Goldberg, Alfred"},{"last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"},{"last_name":"Fraga","first_name":"Hugo","full_name":"Fraga, Hugo"}],"article_processing_charge":"No","article_type":"original","publication":"Journal of Biological Chemistry","_id":"8440","year":"2018","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"American Society for Biochemistry & Molecular Biology"},{"day":"13","author":[{"last_name":"Samanta","first_name":"Dipak","full_name":"Samanta, Dipak"},{"last_name":"Galaktionova","first_name":"Daria","full_name":"Galaktionova, Daria"},{"first_name":"Julius","last_name":"Gemen","full_name":"Gemen, Julius"},{"full_name":"Shimon, Linda J. W.","last_name":"Shimon","first_name":"Linda J. W."},{"first_name":"Yael","last_name":"Diskin-Posner","full_name":"Diskin-Posner, Yael"},{"full_name":"Avram, Liat","first_name":"Liat","last_name":"Avram"},{"last_name":"Král","first_name":"Petr","full_name":"Král, Petr"},{"first_name":"Rafal","last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","full_name":"Klajn, Rafal"}],"title":"Reversible chromism of spiropyran in the cavity of a flexible coordination cage","article_number":"641","pmid":1,"publisher":"Springer Nature","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":"1","article_processing_charge":"No","article_type":"original","publication":"Nature Communications","publication_identifier":{"eissn":["2041-1723"]},"quality_controlled":"1","doi":"10.1038/s41467-017-02715-6","language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"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"}],"date_updated":"2023-08-07T10:54:05Z","month":"02","type":"journal_article","oa_version":"Published Version","date_created":"2023-08-01T09:39:32Z","volume":9,"year":"2018","_id":"13374","oa":1,"publication_status":"published","main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-02715-6","open_access":"1"}],"date_published":"2018-02-13T00:00:00Z","external_id":{"pmid":["29440687"]},"status":"public","citation":{"ama":"Samanta D, Galaktionova D, Gemen J, et al. Reversible chromism of spiropyran in the cavity of a flexible coordination cage. <i>Nature Communications</i>. 2018;9. doi:<a href=\"https://doi.org/10.1038/s41467-017-02715-6\">10.1038/s41467-017-02715-6</a>","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>.","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>","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.","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>.","short":"D. Samanta, D. Galaktionova, J. Gemen, L.J.W. Shimon, Y. Diskin-Posner, L. Avram, P. Král, R. Klajn, Nature Communications 9 (2018)."},"intvolume":"         9","extern":"1","related_material":{"link":[{"url":"https://doi.org/10.1038/s41467-018-03701-2","relation":"erratum"}]}},{"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"}],"date_updated":"2023-11-07T11:46:12Z","month":"05","type":"journal_article","oa_version":"Published Version","date_created":"2023-09-06T12:07:33Z","volume":9,"year":"2018","_id":"14284","publication_status":"published","oa":1,"main_file_link":[{"url":"https://doi.org/10.1038/s41467-018-04139-2","open_access":"1"}],"date_published":"2018-05-04T00:00:00Z","external_id":{"pmid":["29728606"]},"status":"public","citation":{"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).","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.","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>.","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>.","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.","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>","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>"},"intvolume":"         9","extern":"1","day":"04","author":[{"last_name":"Bräuning","first_name":"Bastian","full_name":"Bräuning, Bastian"},{"first_name":"Eva","last_name":"Bertosin","full_name":"Bertosin, Eva"},{"id":"dfec9381-4341-11ee-8fd8-faa02bba7d62","full_name":"Praetorius, Florian M","last_name":"Praetorius","first_name":"Florian M"},{"full_name":"Ihling, Christian","last_name":"Ihling","first_name":"Christian"},{"full_name":"Schatt, Alexandra","first_name":"Alexandra","last_name":"Schatt"},{"first_name":"Agnes","last_name":"Adler","full_name":"Adler, Agnes"},{"full_name":"Richter, Klaus","last_name":"Richter","first_name":"Klaus"},{"full_name":"Sinz, Andrea","first_name":"Andrea","last_name":"Sinz"},{"full_name":"Dietz, Hendrik","first_name":"Hendrik","last_name":"Dietz"},{"full_name":"Groll, Michael","first_name":"Michael","last_name":"Groll"}],"title":"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB","article_number":"1806","pmid":1,"publisher":"Springer Nature","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","scopus_import":"1","article_type":"original","publication":"Nature Communications","publication_identifier":{"issn":["2041-1723"]},"quality_controlled":"1","doi":"10.1038/s41467-018-04139-2","language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"]},{"volume":8,"date_created":"2022-04-07T07:45:50Z","date_updated":"2022-07-18T08:33:03Z","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."}],"type":"journal_article","month":"08","oa_version":"Published Version","_id":"11065","year":"2017","date_published":"2017-08-30T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-00322-z","open_access":"1"}],"oa":1,"publication_status":"published","intvolume":"         8","extern":"1","citation":{"short":"A. Buchwalter, M. Hetzer, Nature Communications 8 (2017).","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>.","ieee":"A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","apa":"Buchwalter, A., &#38; Hetzer, M. (2017). Nucleolar expansion and elevated protein translation in premature aging. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-017-00322-z\">https://doi.org/10.1038/s41467-017-00322-z</a>","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>.","ista":"Buchwalter A, Hetzer M. 2017. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 8, 328.","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>"},"external_id":{"pmid":["28855503"]},"status":"public","title":"Nucleolar expansion and elevated protein translation in premature aging","article_number":"328","author":[{"last_name":"Buchwalter","first_name":"Abigail","full_name":"Buchwalter, Abigail"},{"first_name":"Martin W","last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"day":"30","publication":"Nature Communications","scopus_import":"1","article_processing_charge":"No","article_type":"original","publisher":"Springer Nature","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","pmid":1,"doi":"10.1038/s41467-017-00322-z","quality_controlled":"1","publication_identifier":{"issn":["2041-1723"]},"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"language":[{"iso":"eng"}]},{"article_type":"original","article_processing_charge":"No","scopus_import":"1","publication":"Nature Communications","pmid":1,"publisher":"Springer Nature","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_number":"15651","title":"Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering","day":"15","author":[{"last_name":"Walt","first_name":"Samuel G.","full_name":"Walt, Samuel G."},{"first_name":"Niraghatam","last_name":"Bhargava Ram","full_name":"Bhargava Ram, Niraghatam"},{"last_name":"Atala","first_name":"Marcos","full_name":"Atala, Marcos"},{"full_name":"Shvetsov-Shilovski, Nikolay I","last_name":"Shvetsov-Shilovski","first_name":"Nikolay I"},{"full_name":"von Conta, Aaron","last_name":"von Conta","first_name":"Aaron"},{"last_name":"Baykusheva","first_name":"Denitsa Rangelova","full_name":"Baykusheva, Denitsa Rangelova","id":"71b4d059-2a03-11ee-914d-dfa3beed6530"},{"first_name":"Manfred","last_name":"Lein","full_name":"Lein, Manfred"},{"first_name":"Hans Jakob","last_name":"Wörner","full_name":"Wörner, Hans Jakob"}],"language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"quality_controlled":"1","doi":"10.1038/ncomms15651","publication_identifier":{"eissn":["2041-1723"]},"_id":"14005","year":"2017","date_created":"2023-08-10T06:36:09Z","volume":8,"oa_version":"Published Version","type":"journal_article","month":"06","date_updated":"2023-08-22T08:26:06Z","abstract":[{"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.","lang":"eng"}],"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>","mla":"Walt, Samuel G., et al. “Dynamics of Valence-Shell Electrons and Nuclei Probed by Strong-Field Holography and Rescattering.” <i>Nature Communications</i>, vol. 8, 15651, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/ncomms15651\">10.1038/ncomms15651</a>.","ista":"Walt SG, Bhargava Ram N, Atala M, Shvetsov-Shilovski NI, von Conta A, Baykusheva DR, Lein M, Wörner HJ. 2017. Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. Nature Communications. 8, 15651.","ama":"Walt SG, Bhargava Ram N, Atala M, et al. Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. <i>Nature Communications</i>. 2017;8. doi:<a href=\"https://doi.org/10.1038/ncomms15651\">10.1038/ncomms15651</a>","short":"S.G. Walt, N. Bhargava Ram, M. Atala, N.I. Shvetsov-Shilovski, A. von Conta, D.R. Baykusheva, M. Lein, H.J. Wörner, Nature Communications 8 (2017).","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>.","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."},"extern":"1","intvolume":"         8","status":"public","external_id":{"pmid":["28643771"]},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms15651"}],"date_published":"2017-06-15T00:00:00Z","oa":1,"publication_status":"published"},{"_id":"10370","year":"2017","date_created":"2021-11-29T08:51:38Z","file_date_updated":"2021-11-29T09:07:41Z","volume":6,"date_updated":"2021-11-29T09:28:14Z","abstract":[{"text":"Eukaryotic cells are densely packed with macromolecular complexes and intertwining organelles, continually transported and reshaped. Intriguingly, organelles avoid clashing and entangling with each other in such limited space. Mitochondria form extensive networks constantly remodeled by fission and fusion. Here, we show that mitochondrial fission is triggered by mechanical forces. Mechano-stimulation of mitochondria – via encounter with motile intracellular pathogens, via external pressure applied by an atomic force microscope, or via cell migration across uneven microsurfaces – results in the recruitment of the mitochondrial fission machinery, and subsequent division. We propose that MFF, owing to affinity for narrow mitochondria, acts as a membrane-bound force sensor to recruit the fission machinery to mechanically strained sites. Thus, mitochondria adapt to the environment by sensing and responding to biomechanical cues. Our findings that mechanical triggers can be coupled to biochemical responses in membrane dynamics may explain how organelles orderly cohabit in the crowded cytoplasm.","lang":"eng"}],"month":"11","oa_version":"Published Version","type":"journal_article","citation":{"ama":"Helle SCJ, Feng Q, Aebersold MJ, et al. Mechanical force induces mitochondrial fission. <i>eLife</i>. 2017;6. doi:<a href=\"https://doi.org/10.7554/elife.30292\">10.7554/elife.30292</a>","apa":"Helle, S. C. J., Feng, Q., Aebersold, M. J., Hirt, L., Grüter, R. R., Vahid, A., … Kornmann, B. (2017). Mechanical force induces mitochondrial fission. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/elife.30292\">https://doi.org/10.7554/elife.30292</a>","ista":"Helle SCJ, Feng Q, Aebersold MJ, Hirt L, Grüter RR, Vahid A, Sirianni A, Mostowy S, Snedeker JG, Šarić A, Idema T, Zambelli T, Kornmann B. 2017. Mechanical force induces mitochondrial fission. eLife. 6, e30292.","mla":"Helle, Sebastian Carsten Johannes, et al. “Mechanical Force Induces Mitochondrial Fission.” <i>ELife</i>, vol. 6, e30292, eLife Sciences Publications, 2017, doi:<a href=\"https://doi.org/10.7554/elife.30292\">10.7554/elife.30292</a>.","chicago":"Helle, Sebastian Carsten Johannes, Qian Feng, Mathias J Aebersold, Luca Hirt, Raphael R Grüter, Afshin Vahid, Andrea Sirianni, et al. “Mechanical Force Induces Mitochondrial Fission.” <i>ELife</i>. eLife Sciences Publications, 2017. <a href=\"https://doi.org/10.7554/elife.30292\">https://doi.org/10.7554/elife.30292</a>.","ieee":"S. C. J. Helle <i>et al.</i>, “Mechanical force induces mitochondrial fission,” <i>eLife</i>, vol. 6. eLife Sciences Publications, 2017.","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)."},"extern":"1","intvolume":"         6","status":"public","external_id":{"pmid":["29119945"]},"main_file_link":[{"url":"https://elifesciences.org/articles/30292","open_access":"1"}],"ddc":["572"],"date_published":"2017-11-09T00:00:00Z","has_accepted_license":"1","oa":1,"publication_status":"published","article_processing_charge":"No","scopus_import":"1","article_type":"original","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"publication":"eLife","pmid":1,"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","publisher":"eLife Sciences Publications","title":"Mechanical force induces mitochondrial fission","article_number":"e30292","file":[{"content_type":"application/pdf","relation":"main_file","file_size":6120157,"creator":"cchlebak","success":1,"file_name":"2017_eLife_Helle.pdf","date_created":"2021-11-29T09:07:41Z","access_level":"open_access","date_updated":"2021-11-29T09:07:41Z","file_id":"10372","checksum":"c35f42dcfb007f6d6c761a27e24c26d3"}],"day":"09","author":[{"last_name":"Helle","first_name":"Sebastian Carsten Johannes","full_name":"Helle, Sebastian Carsten Johannes"},{"first_name":"Qian","last_name":"Feng","full_name":"Feng, Qian"},{"first_name":"Mathias J","last_name":"Aebersold","full_name":"Aebersold, Mathias J"},{"last_name":"Hirt","first_name":"Luca","full_name":"Hirt, Luca"},{"last_name":"Grüter","first_name":"Raphael R","full_name":"Grüter, Raphael R"},{"first_name":"Afshin","last_name":"Vahid","full_name":"Vahid, Afshin"},{"full_name":"Sirianni, Andrea","last_name":"Sirianni","first_name":"Andrea"},{"full_name":"Mostowy, Serge","last_name":"Mostowy","first_name":"Serge"},{"full_name":"Snedeker, Jess G","last_name":"Snedeker","first_name":"Jess G"},{"full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","first_name":"Anđela","last_name":"Šarić"},{"full_name":"Idema, Timon","first_name":"Timon","last_name":"Idema"},{"last_name":"Zambelli","first_name":"Tomaso","full_name":"Zambelli, Tomaso"},{"full_name":"Kornmann, Benoît","first_name":"Benoît","last_name":"Kornmann"}],"language":[{"iso":"eng"}],"keyword":["general immunology and microbiology","general biochemistry","genetics and molecular biology","general medicine","general neuroscience"],"quality_controlled":"1","doi":"10.7554/elife.30292","publication_identifier":{"issn":["2050-084X"]}},{"related_material":{"link":[{"url":"https://doi.org/10.1038/ncomms16030","relation":"erratum"}]},"extern":"1","intvolume":"         7","citation":{"chicago":"Ven, Robert A.H. van de, Jolien S. de Groot, Danielle Park, Robert van Domselaar, Danielle de Jong, Karoly Szuhai, Elsken van der Wall, et al. “P120-Catenin Prevents Multinucleation through Control of MKLP1-Dependent RhoA Activity during Cytokinesis.” <i>Nature Communications</i>. Springer Nature, 2016. <a href=\"https://doi.org/10.1038/ncomms13874\">https://doi.org/10.1038/ncomms13874</a>.","ieee":"R. A. H. van de Ven <i>et al.</i>, “p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis,” <i>Nature Communications</i>, vol. 7. Springer Nature, 2016.","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>","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>","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."},"external_id":{"pmid":["28004812"]},"status":"public","date_published":"2016-12-22T00:00:00Z","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms13874"}],"publication_status":"published","oa":1,"_id":"11072","year":"2016","volume":7,"date_created":"2022-04-07T07:48:34Z","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"}],"date_updated":"2022-07-18T08:34:32Z","oa_version":"Published Version","month":"12","type":"journal_article","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"language":[{"iso":"eng"}],"doi":"10.1038/ncomms13874","quality_controlled":"1","publication_identifier":{"issn":["2041-1723"]},"publication":"Nature Communications","scopus_import":"1","article_processing_charge":"No","article_type":"original","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publisher":"Springer Nature","pmid":1,"title":"p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis","article_number":"13874","author":[{"first_name":"Robert A.H.","last_name":"van de Ven","full_name":"van de Ven, Robert A.H."},{"last_name":"de Groot","first_name":"Jolien S.","full_name":"de Groot, Jolien S."},{"first_name":"Danielle","last_name":"Park","full_name":"Park, Danielle"},{"full_name":"van Domselaar, Robert","first_name":"Robert","last_name":"van Domselaar"},{"last_name":"de Jong","first_name":"Danielle","full_name":"de Jong, Danielle"},{"last_name":"Szuhai","first_name":"Karoly","full_name":"Szuhai, Karoly"},{"full_name":"van der Wall, Elsken","last_name":"van der Wall","first_name":"Elsken"},{"first_name":"Oscar M.","last_name":"Rueda","full_name":"Rueda, Oscar M."},{"last_name":"Ali","first_name":"H. Raza","full_name":"Ali, H. Raza"},{"full_name":"Caldas, Carlos","first_name":"Carlos","last_name":"Caldas"},{"full_name":"van Diest, Paul J.","last_name":"van Diest","first_name":"Paul J."},{"first_name":"Martin W","last_name":"HETZER","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"},{"last_name":"Sahai","first_name":"Erik","full_name":"Sahai, Erik"},{"first_name":"Patrick W.B.","last_name":"Derksen","full_name":"Derksen, Patrick W.B."}],"day":"22"},{"doi":"10.1016/j.cell.2015.06.005","quality_controlled":"1","publication_identifier":{"issn":["0092-8674"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"issue":"7","language":[{"iso":"eng"}],"title":"Linking micronuclei to chromosome fragmentation","author":[{"first_name":"Emily M.","last_name":"Hatch","full_name":"Hatch, Emily M."},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER"}],"day":"18","publication":"Cell","article_type":"original","article_processing_charge":"No","scopus_import":"1","publisher":"Elsevier","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","pmid":1,"date_published":"2015-06-18T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2015.06.005","open_access":"1"}],"oa":1,"publication_status":"published","intvolume":"       161","extern":"1","citation":{"chicago":"Hatch, Emily M., and Martin Hetzer. “Linking Micronuclei to Chromosome Fragmentation.” <i>Cell</i>. Elsevier, 2015. <a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">https://doi.org/10.1016/j.cell.2015.06.005</a>.","ieee":"E. M. Hatch and M. Hetzer, “Linking micronuclei to chromosome fragmentation,” <i>Cell</i>, vol. 161, no. 7. Elsevier, pp. 1502–1504, 2015.","short":"E.M. Hatch, M. Hetzer, Cell 161 (2015) 1502–1504.","ama":"Hatch EM, Hetzer M. Linking micronuclei to chromosome fragmentation. <i>Cell</i>. 2015;161(7):1502-1504. doi:<a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">10.1016/j.cell.2015.06.005</a>","apa":"Hatch, E. M., &#38; Hetzer, M. (2015). Linking micronuclei to chromosome fragmentation. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">https://doi.org/10.1016/j.cell.2015.06.005</a>","mla":"Hatch, Emily M., and Martin Hetzer. “Linking Micronuclei to Chromosome Fragmentation.” <i>Cell</i>, vol. 161, no. 7, Elsevier, 2015, pp. 1502–04, doi:<a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">10.1016/j.cell.2015.06.005</a>.","ista":"Hatch EM, Hetzer M. 2015. Linking micronuclei to chromosome fragmentation. Cell. 161(7), 1502–1504."},"status":"public","external_id":{"pmid":["26091034"]},"volume":161,"date_created":"2022-04-07T07:48:49Z","page":"1502-1504","month":"06","type":"journal_article","oa_version":"Published Version","abstract":[{"text":"Human cancer cells bear complex chromosome rearrangements that can be potential drivers of cancer development. However, the molecular mechanisms underlying these rearrangements have been unclear. Zhang et al. use a new technique combining live-cell imaging and single-cell sequencing to demonstrate that chromosomes mis-segregated to micronuclei frequently undergo chromothripsis-like rearrangements in the subsequent cell cycle.","lang":"eng"}],"date_updated":"2022-07-18T08:34:33Z","_id":"11073","year":"2015"},{"doi":"10.1016/j.cub.2015.02.033","quality_controlled":"1","publication_identifier":{"issn":["0960-9822"]},"keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"issue":"10","title":"Chromothripsis","author":[{"full_name":"Hatch, Emily M.","first_name":"Emily M.","last_name":"Hatch"},{"first_name":"Martin W","last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"day":"18","publication":"Current Biology","article_processing_charge":"No","scopus_import":"1","article_type":"original","publisher":"Elsevier","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","pmid":1,"date_published":"2015-05-18T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1016/j.cub.2015.02.033","open_access":"1"}],"publication_status":"published","oa":1,"intvolume":"        25","extern":"1","citation":{"short":"E.M. Hatch, M. Hetzer, Current Biology 25 (2015) PR397-R399.","ieee":"E. M. Hatch and M. Hetzer, “Chromothripsis,” <i>Current Biology</i>, vol. 25, no. 10. Elsevier, pp. PR397-R399, 2015.","chicago":"Hatch, Emily M., and Martin Hetzer. “Chromothripsis.” <i>Current Biology</i>. Elsevier, 2015. <a href=\"https://doi.org/10.1016/j.cub.2015.02.033\">https://doi.org/10.1016/j.cub.2015.02.033</a>.","mla":"Hatch, Emily M., and Martin Hetzer. “Chromothripsis.” <i>Current Biology</i>, vol. 25, no. 10, Elsevier, 2015, pp. PR397-R399, doi:<a href=\"https://doi.org/10.1016/j.cub.2015.02.033\">10.1016/j.cub.2015.02.033</a>.","ista":"Hatch EM, Hetzer M. 2015. Chromothripsis. Current Biology. 25(10), PR397-R399.","apa":"Hatch, E. M., &#38; Hetzer, M. (2015). Chromothripsis. <i>Current Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cub.2015.02.033\">https://doi.org/10.1016/j.cub.2015.02.033</a>","ama":"Hatch EM, Hetzer M. Chromothripsis. <i>Current Biology</i>. 2015;25(10):PR397-R399. doi:<a href=\"https://doi.org/10.1016/j.cub.2015.02.033\">10.1016/j.cub.2015.02.033</a>"},"status":"public","external_id":{"pmid":["25989073"]},"volume":25,"date_created":"2022-04-07T07:49:00Z","page":"PR397-R399","date_updated":"2022-07-18T08:34:34Z","month":"05","type":"journal_article","oa_version":"Published Version","_id":"11074","year":"2015"}]