[{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"extern":"1","external_id":{"pmid":["31217444"]},"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"}],"date_created":"2020-09-17T10:28:25Z","publication":"Nature Communications","year":"2019","date_updated":"2021-01-12T08:19:03Z","publication_identifier":{"issn":["2041-1723"]},"_id":"8405","type":"journal_article","intvolume":"        10","pmid":1,"date_published":"2019-06-19T00:00:00Z","article_processing_charge":"No","title":"Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex","language":[{"iso":"eng"}],"volume":10,"publisher":"Springer Nature","day":"19","author":[{"last_name":"Gauto","full_name":"Gauto, Diego F.","first_name":"Diego F."},{"first_name":"Leandro F.","full_name":"Estrozi, Leandro F.","last_name":"Estrozi"},{"last_name":"Schwieters","full_name":"Schwieters, Charles D.","first_name":"Charles D."},{"full_name":"Effantin, Gregory","last_name":"Effantin","first_name":"Gregory"},{"last_name":"Macek","full_name":"Macek, Pavel","first_name":"Pavel"},{"full_name":"Sounier, Remy","last_name":"Sounier","first_name":"Remy"},{"full_name":"Sivertsen, Astrid C.","last_name":"Sivertsen","first_name":"Astrid C."},{"full_name":"Schmidt, Elena","last_name":"Schmidt","first_name":"Elena"},{"first_name":"Rime","last_name":"Kerfah","full_name":"Kerfah, Rime"},{"first_name":"Guillaume","full_name":"Mas, Guillaume","last_name":"Mas"},{"first_name":"Jacques-Philippe","last_name":"Colletier","full_name":"Colletier, Jacques-Philippe"},{"first_name":"Peter","full_name":"Güntert, Peter","last_name":"Güntert"},{"full_name":"Favier, Adrien","last_name":"Favier","first_name":"Adrien"},{"first_name":"Guy","last_name":"Schoehn","full_name":"Schoehn, Guy"},{"orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","full_name":"Schanda, Paul"},{"first_name":"Jerome","full_name":"Boisbouvier, Jerome","last_name":"Boisbouvier"}],"publication_status":"published","citation":{"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.","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>","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>.","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>.","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.","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).","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>"},"article_number":"2697","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-019-10490-9"}],"status":"public","oa_version":"Published Version","month":"06","article_type":"original","doi":"10.1038/s41467-019-10490-9","quality_controlled":"1"},{"author":[{"first_name":"Sophie","last_name":"Ramananarivo","full_name":"Ramananarivo, Sophie"},{"last_name":"Ducrot","full_name":"Ducrot, Etienne","first_name":"Etienne"},{"last_name":"Palacci","full_name":"Palacci, Jérémie A","orcid":"0000-0002-7253-9465","first_name":"Jérémie A","id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d"}],"day":"29","publisher":"Springer Nature","volume":10,"citation":{"chicago":"Ramananarivo, Sophie, Etienne Ducrot, and Jérémie A Palacci. “Activity-Controlled Annealing of Colloidal Monolayers.” <i>Nature Communications</i>. Springer Nature, 2019. <a href=\"https://doi.org/10.1038/s41467-019-11362-y\">https://doi.org/10.1038/s41467-019-11362-y</a>.","mla":"Ramananarivo, Sophie, et al. “Activity-Controlled Annealing of Colloidal Monolayers.” <i>Nature Communications</i>, vol. 10, no. 1, 3380, Springer Nature, 2019, doi:<a href=\"https://doi.org/10.1038/s41467-019-11362-y\">10.1038/s41467-019-11362-y</a>.","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>","ista":"Ramananarivo S, Ducrot E, Palacci JA. 2019. Activity-controlled annealing of colloidal monolayers. Nature Communications. 10(1), 3380.","short":"S. Ramananarivo, E. Ducrot, J.A. Palacci, Nature Communications 10 (2019).","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>","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."},"file":[{"success":1,"checksum":"70c6e5d6fbea0932b0669505ab6633ec","creator":"cziletti","file_id":"9061","date_updated":"2021-02-02T13:47:21Z","date_created":"2021-02-02T13:47:21Z","content_type":"application/pdf","relation":"main_file","access_level":"open_access","file_size":2820337,"file_name":"2019_NatureComm_Ramananarivo.pdf"}],"publication_status":"published","scopus_import":"1","month":"07","article_type":"original","oa_version":"Published Version","status":"public","issue":"1","ddc":["530"],"article_number":"3380","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"doi":"10.1038/s41467-019-11362-y","quality_controlled":"1","extern":"1","user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","oa":1,"publication_identifier":{"issn":["2041-1723"]},"arxiv":1,"publication":"Nature Communications","date_created":"2021-02-02T13:43:36Z","date_updated":"2023-02-23T13:47:59Z","year":"2019","abstract":[{"lang":"eng","text":"Molecular motors are essential to the living, generating fluctuations that boost transport and assist assembly. Active colloids, that consume energy to move, hold similar potential for man-made materials controlled by forces generated from within. Yet, their use as a powerhouse in materials science lacks. Here we show a massive acceleration of the annealing of a monolayer of passive beads by moderate addition of self-propelled microparticles. We rationalize our observations with a model of collisions that drive active fluctuations and activate the annealing. The experiment is quantitatively compared with Brownian dynamic simulations that further unveil a dynamical transition in the mechanism of annealing. Active dopants travel uniformly in the system or co-localize at the grain boundaries as a result of the persistence of their motion. Our findings uncover the potential of internal activity to control materials and lay the groundwork for the rise of materials science beyond equilibrium."}],"external_id":{"pmid":["31358762"],"arxiv":["1909.07382"]},"intvolume":"        10","_id":"9060","type":"journal_article","has_accepted_license":"1","language":[{"iso":"eng"}],"file_date_updated":"2021-02-02T13:47:21Z","title":"Activity-controlled annealing of colloidal monolayers","article_processing_charge":"No","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"pmid":1,"date_published":"2019-07-29T00:00:00Z"},{"intvolume":"         9","type":"journal_article","_id":"13374","language":[{"iso":"eng"}],"pmid":1,"date_published":"2018-02-13T00:00:00Z","article_processing_charge":"No","title":"Reversible chromism of spiropyran in the cavity of a flexible coordination cage","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"publication":"Nature Communications","date_created":"2023-08-01T09:39:32Z","year":"2018","date_updated":"2024-10-14T12:14:34Z","publication_identifier":{"eissn":["2041-1723"]},"external_id":{"pmid":["29440687"]},"abstract":[{"lang":"eng","text":"Confining molecules to volumes only slightly larger than the molecules themselves can profoundly alter their properties. Molecular switches—entities that can be toggled between two or more forms upon exposure to an external stimulus—often require conformational freedom to isomerize. Therefore, placing these switches in confined spaces can render them non-operational. To preserve the switchability of these species under confinement, we work with a water-soluble coordination cage that is flexible enough to adapt its shape to the conformation of the encapsulated guest. We show that owing to its flexibility, the cage is not only capable of accommodating—and solubilizing in water—several light-responsive spiropyran-based molecular switches, but, more importantly, it also provides an environment suitable for the efficient, reversible photoisomerization of the bound guests. Our findings pave the way towards studying various molecular switching processes in confined environments."}],"oa_version":"Published Version","month":"02","article_type":"original","article_number":"641","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-017-02715-6"}],"status":"public","quality_controlled":"1","doi":"10.1038/s41467-017-02715-6","day":"13","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/s41467-018-03701-2"}]},"author":[{"first_name":"Dipak","full_name":"Samanta, Dipak","last_name":"Samanta"},{"first_name":"Daria","full_name":"Galaktionova, Daria","last_name":"Galaktionova"},{"first_name":"Julius","full_name":"Gemen, Julius","last_name":"Gemen"},{"first_name":"Linda J. W.","last_name":"Shimon","full_name":"Shimon, Linda J. W."},{"first_name":"Yael","last_name":"Diskin-Posner","full_name":"Diskin-Posner, Yael"},{"full_name":"Avram, Liat","last_name":"Avram","first_name":"Liat"},{"full_name":"Král, Petr","last_name":"Král","first_name":"Petr"},{"full_name":"Klajn, Rafal","last_name":"Klajn","first_name":"Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"volume":9,"publisher":"Springer Nature","publication_status":"published","citation":{"ieee":"D. Samanta <i>et al.</i>, “Reversible chromism of spiropyran in the cavity of a flexible coordination cage,” <i>Nature Communications</i>, vol. 9. Springer Nature, 2018.","short":"D. Samanta, D. Galaktionova, J. Gemen, L.J.W. Shimon, Y. Diskin-Posner, L. Avram, P. Král, R. Klajn, Nature Communications 9 (2018).","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>","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>","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>.","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.","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>."},"scopus_import":"1"},{"doi":"10.1038/s41467-018-04139-2","quality_controlled":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-018-04139-2"}],"status":"public","article_number":"1806","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"article_type":"original","month":"05","oa_version":"Published Version","scopus_import":"1","citation":{"ieee":"B. Bräuning <i>et al.</i>, “Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB,” <i>Nature Communications</i>, vol. 9. Springer Nature, 2018.","apa":"Bräuning, B., Bertosin, E., Praetorius, F. M., Ihling, C., Schatt, A., Adler, A., … Groll, M. (2018). Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>","short":"B. Bräuning, E. Bertosin, F.M. Praetorius, C. Ihling, A. Schatt, A. Adler, K. Richter, A. Sinz, H. Dietz, M. Groll, Nature Communications 9 (2018).","mla":"Bräuning, Bastian, et al. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” <i>Nature Communications</i>, vol. 9, 1806, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41467-018-04139-2\">10.1038/s41467-018-04139-2</a>.","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>","chicago":"Bräuning, Bastian, Eva Bertosin, Florian M Praetorius, Christian Ihling, Alexandra Schatt, Agnes Adler, Klaus Richter, Andrea Sinz, Hendrik Dietz, and Michael Groll. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” <i>Nature Communications</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>.","ista":"Bräuning B, Bertosin E, Praetorius FM, Ihling C, Schatt A, Adler A, Richter K, Sinz A, Dietz H, Groll M. 2018. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. Nature Communications. 9, 1806."},"publication_status":"published","publisher":"Springer Nature","volume":9,"author":[{"full_name":"Bräuning, Bastian","last_name":"Bräuning","first_name":"Bastian"},{"first_name":"Eva","last_name":"Bertosin","full_name":"Bertosin, Eva"},{"first_name":"Florian M","id":"dfec9381-4341-11ee-8fd8-faa02bba7d62","full_name":"Praetorius, Florian M","last_name":"Praetorius"},{"last_name":"Ihling","full_name":"Ihling, Christian","first_name":"Christian"},{"first_name":"Alexandra","full_name":"Schatt, Alexandra","last_name":"Schatt"},{"first_name":"Agnes","last_name":"Adler","full_name":"Adler, Agnes"},{"first_name":"Klaus","last_name":"Richter","full_name":"Richter, Klaus"},{"last_name":"Sinz","full_name":"Sinz, Andrea","first_name":"Andrea"},{"first_name":"Hendrik","last_name":"Dietz","full_name":"Dietz, Hendrik"},{"last_name":"Groll","full_name":"Groll, Michael","first_name":"Michael"}],"day":"04","title":"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB","article_processing_charge":"No","date_published":"2018-05-04T00:00:00Z","pmid":1,"language":[{"iso":"eng"}],"type":"journal_article","_id":"14284","intvolume":"         9","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"}],"external_id":{"pmid":["29728606"]},"publication_identifier":{"issn":["2041-1723"]},"date_updated":"2023-11-07T11:46:12Z","year":"2018","publication":"Nature Communications","date_created":"2023-09-06T12:07:33Z","oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1"},{"status":"public","_id":"8436","type":"journal_article","keyword":["General Biochemistry","Genetics and Molecular Biology"],"issue":"5","article_type":"original","month":"11","intvolume":"       175","oa_version":"None","article_processing_charge":"No","title":"Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space","date_published":"2018-11-15T00:00:00Z","doi":"10.1016/j.cell.2018.10.039","quality_controlled":"1","language":[{"iso":"eng"}],"publisher":"Elsevier","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","volume":175,"author":[{"first_name":"Katharina","last_name":"Weinhäupl","full_name":"Weinhäupl, Katharina"},{"first_name":"Caroline","last_name":"Lindau","full_name":"Lindau, Caroline"},{"last_name":"Hessel","full_name":"Hessel, Audrey","first_name":"Audrey"},{"last_name":"Wang","full_name":"Wang, Yong","first_name":"Yong"},{"first_name":"Conny","last_name":"Schütze","full_name":"Schütze, Conny"},{"last_name":"Jores","full_name":"Jores, Tobias","first_name":"Tobias"},{"first_name":"Laura","last_name":"Melchionda","full_name":"Melchionda, Laura"},{"first_name":"Birgit","full_name":"Schönfisch, Birgit","last_name":"Schönfisch"},{"last_name":"Kalbacher","full_name":"Kalbacher, Hubert","first_name":"Hubert"},{"last_name":"Bersch","full_name":"Bersch, Beate","first_name":"Beate"},{"full_name":"Rapaport, Doron","last_name":"Rapaport","first_name":"Doron"},{"first_name":"Martha","last_name":"Brennich","full_name":"Brennich, Martha"},{"first_name":"Kresten","full_name":"Lindorff-Larsen, Kresten","last_name":"Lindorff-Larsen"},{"full_name":"Wiedemann, Nils","last_name":"Wiedemann","first_name":"Nils"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","full_name":"Schanda, Paul"}],"extern":"1","day":"15","abstract":[{"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.","lang":"eng"}],"citation":{"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.","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>","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.","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>","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>.","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."},"publication_identifier":{"issn":["0092-8674"]},"year":"2018","publication_status":"published","page":"1365-1379.e25","date_updated":"2021-01-12T08:19:15Z","publication":"Cell","date_created":"2020-09-18T10:04:39Z"},{"article_type":"original","month":"08","oa_version":"Published Version","main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-00322-z","open_access":"1"}],"status":"public","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"article_number":"328","quality_controlled":"1","doi":"10.1038/s41467-017-00322-z","author":[{"full_name":"Buchwalter, Abigail","last_name":"Buchwalter","first_name":"Abigail"},{"full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X"}],"day":"30","publisher":"Springer Nature","volume":8,"citation":{"ieee":"A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","ista":"Buchwalter A, Hetzer M. 2017. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 8, 328.","chicago":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” <i>Nature Communications</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1038/s41467-017-00322-z\">https://doi.org/10.1038/s41467-017-00322-z</a>.","mla":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” <i>Nature Communications</i>, vol. 8, 328, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/s41467-017-00322-z\">10.1038/s41467-017-00322-z</a>.","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>","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>","short":"A. Buchwalter, M. Hetzer, Nature Communications 8 (2017)."},"publication_status":"published","scopus_import":"1","intvolume":"         8","type":"journal_article","_id":"11065","language":[{"iso":"eng"}],"article_processing_charge":"No","title":"Nucleolar expansion and elevated protein translation in premature aging","date_published":"2017-08-30T00:00:00Z","pmid":1,"extern":"1","oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["2041-1723"]},"year":"2017","date_updated":"2024-10-14T11:20:12Z","publication":"Nature Communications","date_created":"2022-04-07T07:45:50Z","abstract":[{"lang":"eng","text":"Premature aging disorders provide an opportunity to study the mechanisms that drive aging. In Hutchinson-Gilford progeria syndrome (HGPS), a mutant form of the nuclear scaffold protein lamin A distorts nuclei and sequesters nuclear proteins. We sought to investigate protein homeostasis in this disease. Here, we report a widespread increase in protein turnover in HGPS-derived cells compared to normal cells. We determine that global protein synthesis is elevated as a consequence of activated nucleoli and enhanced ribosome biogenesis in HGPS-derived fibroblasts. Depleting normal lamin A or inducing mutant lamin A expression are each sufficient to drive nucleolar expansion. We further show that nucleolar size correlates with donor age in primary fibroblasts derived from healthy individuals and that ribosomal RNA production increases with age, indicating that nucleolar size and activity can serve as aging biomarkers. While limiting ribosome biogenesis extends lifespan in several systems, we show that increased ribosome biogenesis and activity are a hallmark of premature aging."}],"external_id":{"pmid":["28855503"]}},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"extern":"1","abstract":[{"lang":"eng","text":"Strong-field photoelectron holography and laser-induced electron diffraction (LIED) are two powerful emerging methods for probing the ultrafast dynamics of molecules. However, both of them have remained restricted to static systems and to nuclear dynamics induced by strong-field ionization. Here we extend these promising methods to image purely electronic valence-shell dynamics in molecules using photoelectron holography. In the same experiment, we use LIED and photoelectron holography simultaneously, to observe coupled electronic-rotational dynamics taking place on similar timescales. These results offer perspectives for imaging ultrafast dynamics of molecules on femtosecond to attosecond timescales."}],"external_id":{"pmid":["28643771"]},"publication_identifier":{"eissn":["2041-1723"]},"date_created":"2023-08-10T06:36:09Z","publication":"Nature Communications","year":"2017","date_updated":"2023-08-22T08:26:06Z","type":"journal_article","_id":"14005","intvolume":"         8","title":"Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering","article_processing_charge":"No","pmid":1,"date_published":"2017-06-15T00:00:00Z","language":[{"iso":"eng"}],"publisher":"Springer Nature","volume":8,"author":[{"full_name":"Walt, Samuel G.","last_name":"Walt","first_name":"Samuel G."},{"last_name":"Bhargava Ram","full_name":"Bhargava Ram, Niraghatam","first_name":"Niraghatam"},{"first_name":"Marcos","full_name":"Atala, Marcos","last_name":"Atala"},{"first_name":"Nikolay I","last_name":"Shvetsov-Shilovski","full_name":"Shvetsov-Shilovski, Nikolay I"},{"full_name":"von Conta, Aaron","last_name":"von Conta","first_name":"Aaron"},{"first_name":"Denitsa Rangelova","id":"71b4d059-2a03-11ee-914d-dfa3beed6530","last_name":"Baykusheva","full_name":"Baykusheva, Denitsa Rangelova"},{"last_name":"Lein","full_name":"Lein, Manfred","first_name":"Manfred"},{"last_name":"Wörner","full_name":"Wörner, Hans Jakob","first_name":"Hans Jakob"}],"day":"15","scopus_import":"1","citation":{"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>.","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>.","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>","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.","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>","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).","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."},"publication_status":"published","status":"public","main_file_link":[{"url":"https://doi.org/10.1038/ncomms15651","open_access":"1"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"article_number":"15651","month":"06","article_type":"original","oa_version":"Published Version","doi":"10.1038/ncomms15651","quality_controlled":"1"},{"scopus_import":"1","citation":{"ieee":"J. C. Fong <i>et al.</i>, “Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms,” <i>eLife</i>, vol. 6. eLife Sciences Publications, 2017.","apa":"Fong, J. C., Rogers, A., Michael, A. K., Parsley, N. C., Cornell, W.-C., Lin, Y.-C., … Yildiz, F. H. (2017). Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/elife.26163\">https://doi.org/10.7554/elife.26163</a>","short":"J.C. Fong, A. Rogers, A.K. Michael, N.C. Parsley, W.-C. Cornell, Y.-C. Lin, P.K. Singh, R. Hartmann, K. Drescher, E. Vinogradov, L.E. Dietrich, C.L. Partch, F.H. Yildiz, ELife 6 (2017).","ista":"Fong JC, Rogers A, Michael AK, Parsley NC, Cornell W-C, Lin Y-C, Singh PK, Hartmann R, Drescher K, Vinogradov E, Dietrich LE, Partch CL, Yildiz FH. 2017. Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms. eLife. 6, 26163.","ama":"Fong JC, Rogers A, Michael AK, et al. Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms. <i>eLife</i>. 2017;6. doi:<a href=\"https://doi.org/10.7554/elife.26163\">10.7554/elife.26163</a>","chicago":"Fong, Jiunn CN, Andrew Rogers, Alicia K. Michael, Nicole C Parsley, William-Cole Cornell, Yu-Cheng Lin, Praveen K Singh, et al. “Structural Dynamics of RbmA Governs Plasticity of Vibrio Cholerae Biofilms.” <i>ELife</i>. eLife Sciences Publications, 2017. <a href=\"https://doi.org/10.7554/elife.26163\">https://doi.org/10.7554/elife.26163</a>.","mla":"Fong, Jiunn CN, et al. “Structural Dynamics of RbmA Governs Plasticity of Vibrio Cholerae Biofilms.” <i>ELife</i>, vol. 6, 26163, eLife Sciences Publications, 2017, doi:<a href=\"https://doi.org/10.7554/elife.26163\">10.7554/elife.26163</a>."},"publication_status":"published","publisher":"eLife Sciences Publications","volume":6,"author":[{"full_name":"Fong, Jiunn CN","last_name":"Fong","first_name":"Jiunn CN"},{"last_name":"Rogers","full_name":"Rogers, Andrew","first_name":"Andrew"},{"first_name":"Alicia Kathleen","id":"6437c950-2a03-11ee-914d-d6476dd7b75c","full_name":"Michael, Alicia Kathleen","last_name":"Michael"},{"first_name":"Nicole C","last_name":"Parsley","full_name":"Parsley, Nicole C"},{"full_name":"Cornell, William-Cole","last_name":"Cornell","first_name":"William-Cole"},{"first_name":"Yu-Cheng","full_name":"Lin, Yu-Cheng","last_name":"Lin"},{"first_name":"Praveen K","full_name":"Singh, Praveen K","last_name":"Singh"},{"first_name":"Raimo","last_name":"Hartmann","full_name":"Hartmann, Raimo"},{"first_name":"Knut","last_name":"Drescher","full_name":"Drescher, Knut"},{"last_name":"Vinogradov","full_name":"Vinogradov, Evgeny","first_name":"Evgeny"},{"full_name":"Dietrich, Lars EP","last_name":"Dietrich","first_name":"Lars EP"},{"full_name":"Partch, Carrie L","last_name":"Partch","first_name":"Carrie L"},{"first_name":"Fitnat H","full_name":"Yildiz, Fitnat H","last_name":"Yildiz"}],"day":"01","quality_controlled":"1","doi":"10.7554/elife.26163","main_file_link":[{"url":"https://doi.org/10.7554/eLife.26163","open_access":"1"}],"status":"public","keyword":["General Immunology and Microbiology","General Biochemistry","Genetics and Molecular Biology","General Medicine","General Neuroscience"],"article_number":"26163","article_type":"original","month":"08","oa_version":"Published Version","abstract":[{"lang":"eng","text":"Biofilm formation is critical for the infection cycle of Vibrio cholerae. Vibrio exopolysaccharides (VPS) and the matrix proteins RbmA, Bap1 and RbmC are required for the development of biofilm architecture. We demonstrate that RbmA binds VPS directly and uses a binary structural switch within its first fibronectin type III (FnIII-1) domain to control RbmA structural dynamics and the formation of VPS-dependent higher-order structures. The structural switch in FnIII-1 regulates interactions in trans with the FnIII-2 domain, leading to open (monomeric) or closed (dimeric) interfaces. The ability of RbmA to switch between open and closed states is important for V. cholerae biofilm formation, as RbmA variants with switches that are locked in either of the two states lead to biofilms with altered architecture and structural integrity."}],"external_id":{"pmid":["28762945"]},"publication_identifier":{"issn":["2050-084X"]},"date_updated":"2024-03-25T12:22:54Z","year":"2017","publication":"eLife","date_created":"2024-03-21T07:55:36Z","oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","title":"Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms","article_processing_charge":"Yes","date_published":"2017-08-01T00:00:00Z","pmid":1,"language":[{"iso":"eng"}],"_id":"15154","type":"journal_article","intvolume":"         6"},{"day":"09","author":[{"full_name":"Helle, Sebastian Carsten Johannes","last_name":"Helle","first_name":"Sebastian Carsten Johannes"},{"full_name":"Feng, Qian","last_name":"Feng","first_name":"Qian"},{"full_name":"Aebersold, Mathias J","last_name":"Aebersold","first_name":"Mathias J"},{"first_name":"Luca","full_name":"Hirt, Luca","last_name":"Hirt"},{"first_name":"Raphael R","last_name":"Grüter","full_name":"Grüter, Raphael R"},{"full_name":"Vahid, Afshin","last_name":"Vahid","first_name":"Afshin"},{"full_name":"Sirianni, Andrea","last_name":"Sirianni","first_name":"Andrea"},{"first_name":"Serge","full_name":"Mostowy, Serge","last_name":"Mostowy"},{"last_name":"Snedeker","full_name":"Snedeker, Jess G","first_name":"Jess G"},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","first_name":"Anđela","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","last_name":"Šarić"},{"first_name":"Timon","full_name":"Idema, Timon","last_name":"Idema"},{"first_name":"Tomaso","full_name":"Zambelli, Tomaso","last_name":"Zambelli"},{"full_name":"Kornmann, Benoît","last_name":"Kornmann","first_name":"Benoît"}],"volume":6,"publisher":"eLife Sciences Publications","publication_status":"published","citation":{"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>.","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>","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).","ieee":"S. C. J. Helle <i>et al.</i>, “Mechanical force induces mitochondrial fission,” <i>eLife</i>, vol. 6. eLife Sciences Publications, 2017."},"file":[{"content_type":"application/pdf","date_created":"2021-11-29T09:07:41Z","file_id":"10372","date_updated":"2021-11-29T09:07:41Z","file_name":"2017_eLife_Helle.pdf","relation":"main_file","file_size":6120157,"access_level":"open_access","checksum":"c35f42dcfb007f6d6c761a27e24c26d3","success":1,"creator":"cchlebak"}],"scopus_import":"1","oa_version":"Published Version","article_type":"original","month":"11","article_number":"e30292","keyword":["general immunology and microbiology","general biochemistry","genetics and molecular biology","general medicine","general neuroscience"],"ddc":["572"],"main_file_link":[{"open_access":"1","url":"https://elifesciences.org/articles/30292"}],"status":"public","quality_controlled":"1","doi":"10.7554/elife.30292","extern":"1","oa":1,"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","year":"2017","date_updated":"2021-11-29T09:28:14Z","publication":"eLife","date_created":"2021-11-29T08:51:38Z","publication_identifier":{"issn":["2050-084X"]},"external_id":{"pmid":["29119945"]},"abstract":[{"lang":"eng","text":"Eukaryotic cells are densely packed with macromolecular complexes and intertwining organelles, continually transported and reshaped. Intriguingly, organelles avoid clashing and entangling with each other in such limited space. Mitochondria form extensive networks constantly remodeled by fission and fusion. Here, we show that mitochondrial fission is triggered by mechanical forces. Mechano-stimulation of mitochondria – via encounter with motile intracellular pathogens, via external pressure applied by an atomic force microscope, or via cell migration across uneven microsurfaces – results in the recruitment of the mitochondrial fission machinery, and subsequent division. We propose that MFF, owing to affinity for narrow mitochondria, acts as a membrane-bound force sensor to recruit the fission machinery to mechanically strained sites. Thus, mitochondria adapt to the environment by sensing and responding to biomechanical cues. Our findings that mechanical triggers can be coupled to biochemical responses in membrane dynamics may explain how organelles orderly cohabit in the crowded cytoplasm."}],"intvolume":"         6","has_accepted_license":"1","type":"journal_article","_id":"10370","file_date_updated":"2021-11-29T09:07:41Z","language":[{"iso":"eng"}],"date_published":"2017-11-09T00:00:00Z","pmid":1,"tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"article_processing_charge":"No","title":"Mechanical force induces mitochondrial fission"},{"date_created":"2022-04-07T07:48:34Z","publication":"Nature Communications","date_updated":"2022-07-18T08:34:32Z","year":"2016","publication_identifier":{"issn":["2041-1723"]},"external_id":{"pmid":["28004812"]},"abstract":[{"text":"Spatiotemporal activation of RhoA and actomyosin contraction underpins cellular adhesion and division. Loss of cell–cell adhesion and chromosomal instability are cardinal events that drive tumour progression. Here, we show that p120-catenin (p120) not only controls cell–cell adhesion, but also acts as a critical regulator of cytokinesis. We find that p120 regulates actomyosin contractility through concomitant binding to RhoA and the centralspindlin component MKLP1, independent of cadherin association. In anaphase, p120 is enriched at the cleavage furrow where it binds MKLP1 to spatially control RhoA GTPase cycling. Binding of p120 to MKLP1 during cytokinesis depends on the N-terminal coiled-coil domain of p120 isoform 1A. Importantly, clinical data show that loss of p120 expression is a common event in breast cancer that strongly correlates with multinucleation and adverse patient survival. In summary, our study identifies p120 loss as a driver event of chromosomal instability in cancer.\r\n","lang":"eng"}],"extern":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa":1,"language":[{"iso":"eng"}],"pmid":1,"date_published":"2016-12-22T00:00:00Z","article_processing_charge":"No","title":"p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis","intvolume":"         7","_id":"11072","type":"journal_article","publication_status":"published","citation":{"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.","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>.","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.","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>","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).","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>"},"scopus_import":"1","day":"22","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/ncomms16030"}]},"author":[{"full_name":"van de Ven, Robert A.H.","last_name":"van de Ven","first_name":"Robert A.H."},{"last_name":"de Groot","full_name":"de Groot, Jolien S.","first_name":"Jolien S."},{"last_name":"Park","full_name":"Park, Danielle","first_name":"Danielle"},{"first_name":"Robert","last_name":"van Domselaar","full_name":"van Domselaar, Robert"},{"first_name":"Danielle","last_name":"de Jong","full_name":"de Jong, Danielle"},{"full_name":"Szuhai, Karoly","last_name":"Szuhai","first_name":"Karoly"},{"last_name":"van der Wall","full_name":"van der Wall, Elsken","first_name":"Elsken"},{"first_name":"Oscar M.","last_name":"Rueda","full_name":"Rueda, Oscar M."},{"first_name":"H. Raza","last_name":"Ali","full_name":"Ali, H. Raza"},{"last_name":"Caldas","full_name":"Caldas, Carlos","first_name":"Carlos"},{"first_name":"Paul J.","full_name":"van Diest, Paul J.","last_name":"van Diest"},{"full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"},{"first_name":"Erik","full_name":"Sahai, Erik","last_name":"Sahai"},{"first_name":"Patrick W.B.","last_name":"Derksen","full_name":"Derksen, Patrick W.B."}],"volume":7,"publisher":"Springer Nature","quality_controlled":"1","doi":"10.1038/ncomms13874","oa_version":"Published Version","month":"12","article_type":"original","article_number":"13874","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms13874"}],"status":"public"},{"publisher":"Elsevier","volume":161,"author":[{"first_name":"Emily M.","full_name":"Hatch, Emily M.","last_name":"Hatch"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W"}],"day":"18","scopus_import":"1","citation":{"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.","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>","ista":"Hatch EM, Hetzer M. 2015. Linking micronuclei to chromosome fragmentation. Cell. 161(7), 1502–1504.","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>.","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>","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>."},"publication_status":"published","page":"1502-1504","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2015.06.005"}],"status":"public","keyword":["General Biochemistry","Genetics and Molecular Biology"],"issue":"7","article_type":"original","month":"06","oa_version":"Published Version","quality_controlled":"1","doi":"10.1016/j.cell.2015.06.005","oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","abstract":[{"lang":"eng","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."}],"external_id":{"pmid":["26091034"]},"publication_identifier":{"issn":["0092-8674"]},"date_updated":"2024-10-14T11:22:03Z","year":"2015","publication":"Cell","date_created":"2022-04-07T07:48:49Z","type":"journal_article","_id":"11073","intvolume":"       161","article_processing_charge":"No","title":"Linking micronuclei to chromosome fragmentation","date_published":"2015-06-18T00:00:00Z","pmid":1,"language":[{"iso":"eng"}]},{"date_published":"2015-05-18T00:00:00Z","pmid":1,"title":"Chromothripsis","article_processing_charge":"No","language":[{"iso":"eng"}],"_id":"11074","type":"journal_article","intvolume":"        25","external_id":{"pmid":["25989073"]},"year":"2015","date_updated":"2024-10-14T11:22:15Z","date_created":"2022-04-07T07:49:00Z","publication":"Current Biology","publication_identifier":{"issn":["0960-9822"]},"oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","doi":"10.1016/j.cub.2015.02.033","quality_controlled":"1","keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"issue":"10","main_file_link":[{"url":"https://doi.org/10.1016/j.cub.2015.02.033","open_access":"1"}],"status":"public","oa_version":"Published Version","article_type":"original","month":"05","scopus_import":"1","page":"PR397-R399","publication_status":"published","citation":{"short":"E.M. Hatch, M. Hetzer, Current Biology 25 (2015) 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>","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.","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>.","ieee":"E. M. Hatch and M. Hetzer, “Chromothripsis,” <i>Current Biology</i>, vol. 25, no. 10. Elsevier, pp. PR397-R399, 2015."},"volume":25,"publisher":"Elsevier","day":"18","author":[{"first_name":"Emily M.","full_name":"Hatch, Emily M.","last_name":"Hatch"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W"}]},{"extern":"1","oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"eissn":["2041-1723"]},"date_updated":"2023-08-22T08:52:56Z","year":"2015","date_created":"2023-08-10T06:38:01Z","publication":"Nature Communications","abstract":[{"text":"All attosecond time-resolved measurements have so far relied on the use of intense near-infrared laser pulses. In particular, attosecond streaking, laser-induced electron diffraction and high-harmonic generation all make use of non-perturbative light–matter interactions. Remarkably, the effect of the strong laser field on the studied sample has often been neglected in previous studies. Here we use high-harmonic spectroscopy to measure laser-induced modifications of the electronic structure of molecules. We study high-harmonic spectra of spatially oriented CH3F and CH3Br as generic examples of polar polyatomic molecules. We accurately measure intensity ratios of even and odd-harmonic orders, and of the emission from aligned and unaligned molecules. We show that these robust observables reveal a substantial modification of the molecular electronic structure by the external laser field. Our insights offer new challenges and opportunities for a range of emerging strong-field attosecond spectroscopies.","lang":"eng"}],"external_id":{"pmid":["25940229"]},"intvolume":"         6","type":"journal_article","_id":"14016","language":[{"iso":"eng"}],"title":"Observation of laser-induced electronic structure in oriented polyatomic molecules","article_processing_charge":"No","date_published":"2015-05-05T00:00:00Z","pmid":1,"author":[{"first_name":"P. M.","full_name":"Kraus, P. M.","last_name":"Kraus"},{"first_name":"O. I.","full_name":"Tolstikhin, O. I.","last_name":"Tolstikhin"},{"first_name":"Denitsa Rangelova","id":"71b4d059-2a03-11ee-914d-dfa3beed6530","full_name":"Baykusheva, Denitsa Rangelova","last_name":"Baykusheva"},{"full_name":"Rupenyan, A.","last_name":"Rupenyan","first_name":"A."},{"last_name":"Schneider","full_name":"Schneider, J.","first_name":"J."},{"first_name":"C. Z.","full_name":"Bisgaard, C. Z.","last_name":"Bisgaard"},{"first_name":"T.","last_name":"Morishita","full_name":"Morishita, T."},{"last_name":"Jensen","full_name":"Jensen, F.","first_name":"F."},{"last_name":"Madsen","full_name":"Madsen, L. B.","first_name":"L. B."},{"first_name":"H. J.","full_name":"Wörner, H. J.","last_name":"Wörner"}],"day":"05","publisher":"Springer Nature","volume":6,"citation":{"ieee":"P. M. Kraus <i>et al.</i>, “Observation of laser-induced electronic structure in oriented polyatomic molecules,” <i>Nature Communications</i>, vol. 6. Springer Nature, 2015.","mla":"Kraus, P. M., et al. “Observation of Laser-Induced Electronic Structure in Oriented Polyatomic Molecules.” <i>Nature Communications</i>, vol. 6, 7039, Springer Nature, 2015, doi:<a href=\"https://doi.org/10.1038/ncomms8039\">10.1038/ncomms8039</a>.","ama":"Kraus PM, Tolstikhin OI, Baykusheva DR, et al. Observation of laser-induced electronic structure in oriented polyatomic molecules. <i>Nature Communications</i>. 2015;6. doi:<a href=\"https://doi.org/10.1038/ncomms8039\">10.1038/ncomms8039</a>","chicago":"Kraus, P. M., O. I. Tolstikhin, Denitsa Rangelova Baykusheva, A. Rupenyan, J. Schneider, C. Z. Bisgaard, T. Morishita, F. Jensen, L. B. Madsen, and H. J. Wörner. “Observation of Laser-Induced Electronic Structure in Oriented Polyatomic Molecules.” <i>Nature Communications</i>. Springer Nature, 2015. <a href=\"https://doi.org/10.1038/ncomms8039\">https://doi.org/10.1038/ncomms8039</a>.","ista":"Kraus PM, Tolstikhin OI, Baykusheva DR, Rupenyan A, Schneider J, Bisgaard CZ, Morishita T, Jensen F, Madsen LB, Wörner HJ. 2015. Observation of laser-induced electronic structure in oriented polyatomic molecules. Nature Communications. 6, 7039.","apa":"Kraus, P. M., Tolstikhin, O. I., Baykusheva, D. R., Rupenyan, A., Schneider, J., Bisgaard, C. Z., … Wörner, H. J. (2015). Observation of laser-induced electronic structure in oriented polyatomic molecules. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms8039\">https://doi.org/10.1038/ncomms8039</a>","short":"P.M. Kraus, O.I. Tolstikhin, D.R. Baykusheva, A. Rupenyan, J. Schneider, C.Z. Bisgaard, T. Morishita, F. Jensen, L.B. Madsen, H.J. Wörner, Nature Communications 6 (2015)."},"publication_status":"published","scopus_import":"1","article_type":"original","month":"05","oa_version":"Published Version","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms8039"}],"status":"public","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"article_number":"7039","doi":"10.1038/ncomms8039","quality_controlled":"1"},{"publication_identifier":{"issn":["2041-1723"]},"year":"2015","date_updated":"2025-01-22T14:39:22Z","publication":"Nature Communications","date_created":"2020-09-18T10:07:36Z","abstract":[{"text":"The large majority of three-dimensional structures of biological macromolecules have been determined by X-ray diffraction of crystalline samples. High-resolution structure determination crucially depends on the homogeneity of the protein crystal. Overall ‘rocking’ motion of molecules in the crystal is expected to influence diffraction quality, and such motion may therefore affect the process of solving crystal structures. Yet, so far overall molecular motion has not directly been observed in protein crystals, and the timescale of such dynamics remains unclear. Here we use solid-state NMR, X-ray diffraction methods and μs-long molecular dynamics simulations to directly characterize the rigid-body motion of a protein in different crystal forms. For ubiquitin crystals investigated in this study we determine the range of possible correlation times of rocking motion, 0.1–100 μs. The amplitude of rocking varies from one crystal form to another and is correlated with the resolution obtainable in X-ray diffraction experiments.","lang":"eng"}],"extern":"1","oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","OA_type":"gold","language":[{"iso":"eng"}],"article_processing_charge":"Yes","title":"Observing the overall rocking motion of a protein in a crystal","date_published":"2015-10-05T00:00:00Z","intvolume":"         6","type":"journal_article","_id":"8456","citation":{"ieee":"P. Ma <i>et al.</i>, “Observing the overall rocking motion of a protein in a crystal,” <i>Nature Communications</i>, vol. 6. Springer Nature, 2015.","ama":"Ma P, Xue Y, Coquelle N, et al. Observing the overall rocking motion of a protein in a crystal. <i>Nature Communications</i>. 2015;6. doi:<a href=\"https://doi.org/10.1038/ncomms9361\">10.1038/ncomms9361</a>","mla":"Ma, Peixiang, et al. “Observing the Overall Rocking Motion of a Protein in a Crystal.” <i>Nature Communications</i>, vol. 6, 8361, Springer Nature, 2015, doi:<a href=\"https://doi.org/10.1038/ncomms9361\">10.1038/ncomms9361</a>.","chicago":"Ma, Peixiang, Yi Xue, Nicolas Coquelle, Jens D. Haller, Tairan Yuwen, Isabel Ayala, Oleg Mikhailovskii, et al. “Observing the Overall Rocking Motion of a Protein in a Crystal.” <i>Nature Communications</i>. Springer Nature, 2015. <a href=\"https://doi.org/10.1038/ncomms9361\">https://doi.org/10.1038/ncomms9361</a>.","ista":"Ma P, Xue Y, Coquelle N, Haller JD, Yuwen T, Ayala I, Mikhailovskii O, Willbold D, Colletier J-P, Skrynnikov NR, Schanda P. 2015. Observing the overall rocking motion of a protein in a crystal. Nature Communications. 6, 8361.","apa":"Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., … Schanda, P. (2015). Observing the overall rocking motion of a protein in a crystal. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms9361\">https://doi.org/10.1038/ncomms9361</a>","short":"P. Ma, Y. Xue, N. Coquelle, J.D. Haller, T. Yuwen, I. Ayala, O. Mikhailovskii, D. Willbold, J.-P. Colletier, N.R. Skrynnikov, P. Schanda, Nature Communications 6 (2015)."},"publication_status":"published","scopus_import":"1","author":[{"first_name":"Peixiang","last_name":"Ma","full_name":"Ma, Peixiang"},{"first_name":"Yi","full_name":"Xue, Yi","last_name":"Xue"},{"first_name":"Nicolas","full_name":"Coquelle, Nicolas","last_name":"Coquelle"},{"last_name":"Haller","full_name":"Haller, Jens D.","first_name":"Jens D."},{"first_name":"Tairan","full_name":"Yuwen, Tairan","last_name":"Yuwen"},{"full_name":"Ayala, Isabel","last_name":"Ayala","first_name":"Isabel"},{"last_name":"Mikhailovskii","full_name":"Mikhailovskii, Oleg","first_name":"Oleg"},{"first_name":"Dieter","last_name":"Willbold","full_name":"Willbold, Dieter"},{"full_name":"Colletier, Jacques-Philippe","last_name":"Colletier","first_name":"Jacques-Philippe"},{"first_name":"Nikolai R.","full_name":"Skrynnikov, Nikolai R.","last_name":"Skrynnikov"},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda"}],"day":"05","publisher":"Springer Nature","volume":6,"OA_place":"publisher","quality_controlled":"1","doi":"10.1038/ncomms9361","article_type":"original","month":"10","oa_version":"Published Version","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms9361"}],"status":"public","article_number":"8361","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"]},{"publication_status":"published","page":"868-869","citation":{"ieee":"A. Buchwalter and M. Hetzer, “Nuclear pores set the speed limit for mitosis,” <i>Cell</i>, vol. 156, no. 5. Elsevier, pp. 868–869, 2014.","apa":"Buchwalter, A., &#38; Hetzer, M. (2014). Nuclear pores set the speed limit for mitosis. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">https://doi.org/10.1016/j.cell.2014.02.004</a>","short":"A. Buchwalter, M. Hetzer, Cell 156 (2014) 868–869.","chicago":"Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit for Mitosis.” <i>Cell</i>. Elsevier, 2014. <a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">https://doi.org/10.1016/j.cell.2014.02.004</a>.","mla":"Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit for Mitosis.” <i>Cell</i>, vol. 156, no. 5, Elsevier, 2014, pp. 868–69, doi:<a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">10.1016/j.cell.2014.02.004</a>.","ista":"Buchwalter A, Hetzer M. 2014. Nuclear pores set the speed limit for mitosis. Cell. 156(5), 868–869.","ama":"Buchwalter A, Hetzer M. Nuclear pores set the speed limit for mitosis. <i>Cell</i>. 2014;156(5):868-869. doi:<a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">10.1016/j.cell.2014.02.004</a>"},"scopus_import":"1","day":"27","author":[{"first_name":"Abigail","full_name":"Buchwalter, Abigail","last_name":"Buchwalter"},{"orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","full_name":"HETZER, Martin W"}],"volume":156,"publisher":"Elsevier","doi":"10.1016/j.cell.2014.02.004","quality_controlled":"1","oa_version":"Published Version","article_type":"original","month":"02","keyword":["General Biochemistry","Genetics and Molecular Biology"],"issue":"5","status":"public","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2014.02.004","open_access":"1"}],"year":"2014","date_updated":"2024-10-14T11:23:12Z","date_created":"2022-04-07T07:50:04Z","publication":"Cell","publication_identifier":{"issn":["0092-8674"]},"external_id":{"pmid":["24581486"]},"abstract":[{"lang":"eng","text":"The spindle assembly checkpoint prevents separation of sister chromatids until each kinetochore is attached to the mitotic spindle. Rodriguez-Bravo et al. report that the nuclear pore complex scaffolds spindle assembly checkpoint signaling in interphase, providing a store of inhibitory signals that limits the speed of the subsequent mitosis."}],"extern":"1","oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","language":[{"iso":"eng"}],"date_published":"2014-02-27T00:00:00Z","pmid":1,"article_processing_charge":"No","title":"Nuclear pores set the speed limit for mitosis","intvolume":"       156","type":"journal_article","_id":"11080"},{"status":"public","main_file_link":[{"url":"https://doi.org/10.1038/ncomms4588","open_access":"1"}],"article_number":"3588","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"month":"04","article_type":"original","oa_version":"Published Version","quality_controlled":"1","doi":"10.1038/ncomms4588","publisher":"Springer Nature","volume":5,"author":[{"full_name":"Kundu, Pintu K.","last_name":"Kundu","first_name":"Pintu K."},{"full_name":"Olsen, Gregory L.","last_name":"Olsen","first_name":"Gregory L."},{"last_name":"Kiss","full_name":"Kiss, Vladimir","first_name":"Vladimir"},{"first_name":"Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","full_name":"Klajn, Rafal","last_name":"Klajn"}],"day":"07","scopus_import":"1","citation":{"ieee":"P. K. Kundu, G. L. Olsen, V. Kiss, and R. Klajn, “Nanoporous frameworks exhibiting multiple stimuli responsiveness,” <i>Nature Communications</i>, vol. 5. Springer Nature, 2014.","apa":"Kundu, P. K., Olsen, G. L., Kiss, V., &#38; Klajn, R. (2014). Nanoporous frameworks exhibiting multiple stimuli responsiveness. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms4588\">https://doi.org/10.1038/ncomms4588</a>","short":"P.K. Kundu, G.L. Olsen, V. Kiss, R. Klajn, Nature Communications 5 (2014).","mla":"Kundu, Pintu K., et al. “Nanoporous Frameworks Exhibiting Multiple Stimuli Responsiveness.” <i>Nature Communications</i>, vol. 5, 3588, Springer Nature, 2014, doi:<a href=\"https://doi.org/10.1038/ncomms4588\">10.1038/ncomms4588</a>.","ista":"Kundu PK, Olsen GL, Kiss V, Klajn R. 2014. Nanoporous frameworks exhibiting multiple stimuli responsiveness. Nature Communications. 5, 3588.","chicago":"Kundu, Pintu K., Gregory L. Olsen, Vladimir Kiss, and Rafal Klajn. “Nanoporous Frameworks Exhibiting Multiple Stimuli Responsiveness.” <i>Nature Communications</i>. Springer Nature, 2014. <a href=\"https://doi.org/10.1038/ncomms4588\">https://doi.org/10.1038/ncomms4588</a>.","ama":"Kundu PK, Olsen GL, Kiss V, Klajn R. Nanoporous frameworks exhibiting multiple stimuli responsiveness. <i>Nature Communications</i>. 2014;5. doi:<a href=\"https://doi.org/10.1038/ncomms4588\">10.1038/ncomms4588</a>"},"publication_status":"published","_id":"13402","type":"journal_article","intvolume":"         5","article_processing_charge":"No","title":"Nanoporous frameworks exhibiting multiple stimuli responsiveness","pmid":1,"date_published":"2014-04-07T00:00:00Z","language":[{"iso":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"extern":"1","abstract":[{"lang":"eng","text":"Nanoporous frameworks are polymeric materials built from rigid molecules, which give rise to their nanoporous structures with applications in gas sorption and storage, catalysis and others. Conceptually new applications could emerge, should these beneficial properties be manipulated by external stimuli in a reversible manner. One approach to render nanoporous frameworks responsive to external signals would be to immobilize molecular switches within their nanopores. Although the majority of molecular switches require conformational freedom to isomerize, and switching in the solid state is prohibited, the nanopores may provide enough room for the switches to efficiently isomerize. Here we describe two families of nanoporous materials incorporating the spiropyran molecular switch. These materials exhibit a variety of interesting properties, including reversible photochromism and acidochromism under solvent-free conditions, light-controlled capture and release of metal ions, as well reversible chromism induced by solvation/desolvation."}],"external_id":{"pmid":["24709950"]},"publication_identifier":{"eissn":["2041-1723"]},"publication":"Nature Communications","date_created":"2023-08-01T09:46:27Z","year":"2014","date_updated":"2024-10-14T12:20:30Z"},{"type":"journal_article","_id":"11085","intvolume":"       154","pmid":1,"date_published":"2013-07-03T00:00:00Z","title":"Catastrophic nuclear envelope collapse in cancer cell micronuclei","article_processing_charge":"No","language":[{"iso":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"extern":"1","external_id":{"pmid":["23827674"]},"abstract":[{"lang":"eng","text":"During mitotic exit, missegregated chromosomes can recruit their own nuclear envelope (NE) to form micronuclei (MN). MN have reduced functioning compared to primary nuclei in the same cell, although the two compartments appear to be structurally comparable. Here we show that over 60% of MN undergo an irreversible loss of compartmentalization during interphase due to NE collapse. This disruption of the MN, which is induced by defects in nuclear lamina assembly, drastically reduces nuclear functions and can trigger massive DNA damage. MN disruption is associated with chromatin compaction and invasion of endoplasmic reticulum (ER) tubules into the chromatin. We identified disrupted MN in both major subtypes of human non-small-cell lung cancer, suggesting that disrupted MN could be a useful objective biomarker for genomic instability in solid tumors. Our study shows that NE collapse is a key event underlying MN dysfunction and establishes a link between aberrant NE organization and aneuploidy."}],"publication":"Cell","date_created":"2022-04-07T07:50:51Z","year":"2013","date_updated":"2024-10-14T11:24:29Z","publication_identifier":{"issn":["0092-8674"]},"issue":"1","keyword":["General Biochemistry","Genetics and Molecular Biology"],"main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2013.06.007","open_access":"1"}],"status":"public","oa_version":"Published Version","month":"07","article_type":"original","quality_controlled":"1","doi":"10.1016/j.cell.2013.06.007","volume":154,"publisher":"Elsevier","day":"03","author":[{"last_name":"Hatch","full_name":"Hatch, Emily M.","first_name":"Emily M."},{"first_name":"Andrew H.","last_name":"Fischer","full_name":"Fischer, Andrew H."},{"full_name":"Deerinck, Thomas J.","last_name":"Deerinck","first_name":"Thomas J."},{"last_name":"HETZER","full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"}],"scopus_import":"1","publication_status":"published","page":"47-60","citation":{"ieee":"E. M. Hatch, A. H. Fischer, T. J. Deerinck, and M. Hetzer, “Catastrophic nuclear envelope collapse in cancer cell micronuclei,” <i>Cell</i>, vol. 154, no. 1. Elsevier, pp. 47–60, 2013.","ista":"Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. 2013. Catastrophic nuclear envelope collapse in cancer cell micronuclei. Cell. 154(1), 47–60.","chicago":"Hatch, Emily M., Andrew H. Fischer, Thomas J. Deerinck, and Martin Hetzer. “Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei.” <i>Cell</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">https://doi.org/10.1016/j.cell.2013.06.007</a>.","mla":"Hatch, Emily M., et al. “Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei.” <i>Cell</i>, vol. 154, no. 1, Elsevier, 2013, pp. 47–60, doi:<a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">10.1016/j.cell.2013.06.007</a>.","ama":"Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. Catastrophic nuclear envelope collapse in cancer cell micronuclei. <i>Cell</i>. 2013;154(1):47-60. doi:<a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">10.1016/j.cell.2013.06.007</a>","apa":"Hatch, E. M., Fischer, A. H., Deerinck, T. J., &#38; Hetzer, M. (2013). Catastrophic nuclear envelope collapse in cancer cell micronuclei. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">https://doi.org/10.1016/j.cell.2013.06.007</a>","short":"E.M. Hatch, A.H. Fischer, T.J. Deerinck, M. Hetzer, Cell 154 (2013) 47–60."}},{"day":"29","author":[{"last_name":"Toyama","full_name":"Toyama, Brandon H.","first_name":"Brandon H."},{"last_name":"Savas","full_name":"Savas, Jeffrey N.","first_name":"Jeffrey N."},{"first_name":"Sung Kyu","full_name":"Park, Sung Kyu","last_name":"Park"},{"last_name":"Harris","full_name":"Harris, Michael S.","first_name":"Michael S."},{"last_name":"Ingolia","full_name":"Ingolia, Nicholas T.","first_name":"Nicholas T."},{"last_name":"Yates","full_name":"Yates, John R.","first_name":"John R."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W"}],"volume":154,"publisher":"Elsevier","publication_status":"published","page":"971-982","citation":{"short":"B.H. Toyama, J.N. Savas, S.K. Park, M.S. Harris, N.T. Ingolia, J.R. Yates, M. Hetzer, Cell 154 (2013) 971–982.","apa":"Toyama, B. H., Savas, J. N., Park, S. K., Harris, M. S., Ingolia, N. T., Yates, J. R., &#38; Hetzer, M. (2013). Identification of long-lived proteins reveals exceptional stability of essential cellular structures. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">https://doi.org/10.1016/j.cell.2013.07.037</a>","ista":"Toyama BH, Savas JN, Park SK, Harris MS, Ingolia NT, Yates JR, Hetzer M. 2013. Identification of long-lived proteins reveals exceptional stability of essential cellular structures. Cell. 154(5), 971–982.","chicago":"Toyama, Brandon H., Jeffrey N. Savas, Sung Kyu Park, Michael S. Harris, Nicholas T. Ingolia, John R. Yates, and Martin Hetzer. “Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures.” <i>Cell</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">https://doi.org/10.1016/j.cell.2013.07.037</a>.","ama":"Toyama BH, Savas JN, Park SK, et al. Identification of long-lived proteins reveals exceptional stability of essential cellular structures. <i>Cell</i>. 2013;154(5):971-982. doi:<a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">10.1016/j.cell.2013.07.037</a>","mla":"Toyama, Brandon H., et al. “Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures.” <i>Cell</i>, vol. 154, no. 5, Elsevier, 2013, pp. 971–82, doi:<a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">10.1016/j.cell.2013.07.037</a>.","ieee":"B. H. Toyama <i>et al.</i>, “Identification of long-lived proteins reveals exceptional stability of essential cellular structures,” <i>Cell</i>, vol. 154, no. 5. Elsevier, pp. 971–982, 2013."},"scopus_import":"1","oa_version":"Published Version","month":"08","article_type":"original","issue":"5","keyword":["General Biochemistry","Genetics and Molecular Biology"],"status":"public","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2013.07.037","open_access":"1"}],"doi":"10.1016/j.cell.2013.07.037","quality_controlled":"1","extern":"1","department":[{"_id":"MaHe"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"date_created":"2022-04-07T07:51:08Z","publication":"Cell","date_updated":"2025-12-15T10:02:46Z","year":"2013","publication_identifier":{"issn":["0092-8674"]},"external_id":{"pmid":["23993091"]},"abstract":[{"text":"Intracellular proteins with long lifespans have recently been linked to age-dependent defects, ranging from decreased fertility to the functional decline of neurons. Why long-lived proteins exist in metabolically active cellular environments and how they are maintained over time remains poorly understood. Here, we provide a system-wide identification of proteins with exceptional lifespans in the rat brain. These proteins are inefficiently replenished despite being translated robustly throughout adulthood. Using nucleoporins as a paradigm for long-term protein persistence, we found that nuclear pore complexes (NPCs) are maintained over a cell’s life through slow but finite exchange of even its most stable subcomplexes. This maintenance is limited, however, as some nucleoporin levels decrease during aging, providing a rationale for the previously observed age-dependent deterioration of NPC function. Our identification of a long-lived proteome reveals cellular components that are at increased risk for damage accumulation, linking long-term protein persistence to the cellular aging process.","lang":"eng"}],"intvolume":"       154","_id":"11087","type":"journal_article","language":[{"iso":"eng"}],"pmid":1,"date_published":"2013-08-29T00:00:00Z","article_processing_charge":"No","title":"Identification of long-lived proteins reveals exceptional stability of essential cellular structures"},{"quality_controlled":"1","doi":"10.1016/j.cell.2012.04.018","month":"05","article_type":"letter_note","oa_version":"Published Version","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2012.04.018"}],"issue":"4","keyword":["General Biochemistry","Genetics and Molecular Biology"],"citation":{"short":"E.M. Hatch, M. Hetzer, Cell 149 (2012) 733–735.","apa":"Hatch, E. M., &#38; Hetzer, M. (2012). RNP export by nuclear envelope budding. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">https://doi.org/10.1016/j.cell.2012.04.018</a>","mla":"Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.” <i>Cell</i>, vol. 149, no. 4, Elsevier, 2012, pp. 733–35, doi:<a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">10.1016/j.cell.2012.04.018</a>.","ama":"Hatch EM, Hetzer M. RNP export by nuclear envelope budding. <i>Cell</i>. 2012;149(4):733-735. doi:<a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">10.1016/j.cell.2012.04.018</a>","ista":"Hatch EM, Hetzer M. 2012. RNP export by nuclear envelope budding. Cell. 149(4), 733–735.","chicago":"Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.” <i>Cell</i>. Elsevier, 2012. <a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">https://doi.org/10.1016/j.cell.2012.04.018</a>.","ieee":"E. M. Hatch and M. Hetzer, “RNP export by nuclear envelope budding,” <i>Cell</i>, vol. 149, no. 4. Elsevier, pp. 733–735, 2012."},"page":"733-735","publication_status":"published","scopus_import":"1","author":[{"first_name":"Emily M.","last_name":"Hatch","full_name":"Hatch, Emily M."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"}],"day":"11","publisher":"Elsevier","volume":149,"language":[{"iso":"eng"}],"article_processing_charge":"No","title":"RNP export by nuclear envelope budding","pmid":1,"date_published":"2012-05-11T00:00:00Z","intvolume":"       149","type":"journal_article","_id":"11090","publication_identifier":{"issn":["0092-8674"]},"publication":"Cell","date_created":"2022-04-07T07:51:45Z","year":"2012","date_updated":"2024-10-14T11:25:24Z","abstract":[{"lang":"eng","text":"Nuclear export of mRNAs is thought to occur exclusively through nuclear pore complexes. In this issue of Cell, Speese et al. identify an alternate pathway for mRNA export in muscle cells where ribonucleoprotein complexes involved in forming neuromuscular junctions transit the nuclear envelope by fusing with and budding through the nuclear membrane."}],"external_id":{"pmid":["22579277"]},"extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1},{"publisher":"Elsevier","volume":22,"author":[{"full_name":"D'Angelo, Maximiliano A.","last_name":"D'Angelo","first_name":"Maximiliano A."},{"full_name":"Gomez-Cavazos, J. Sebastian","last_name":"Gomez-Cavazos","first_name":"J. Sebastian"},{"last_name":"Mei","full_name":"Mei, Arianna","first_name":"Arianna"},{"last_name":"Lackner","full_name":"Lackner, Daniel H.","first_name":"Daniel H."},{"full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"}],"day":"19","scopus_import":"1","citation":{"ieee":"M. A. D’Angelo, J. S. Gomez-Cavazos, A. Mei, D. H. Lackner, and M. Hetzer, “A change in nuclear pore complex composition regulates cell differentiation,” <i>Developmental Cell</i>, vol. 22, no. 2. Elsevier, pp. 446–458, 2012.","ista":"D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. 2012. A change in nuclear pore complex composition regulates cell differentiation. Developmental Cell. 22(2), 446–458.","ama":"D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. A change in nuclear pore complex composition regulates cell differentiation. <i>Developmental Cell</i>. 2012;22(2):446-458. doi:<a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">10.1016/j.devcel.2011.11.021</a>","mla":"D’Angelo, Maximiliano A., et al. “A Change in Nuclear Pore Complex Composition Regulates Cell Differentiation.” <i>Developmental Cell</i>, vol. 22, no. 2, Elsevier, 2012, pp. 446–58, doi:<a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">10.1016/j.devcel.2011.11.021</a>.","chicago":"D’Angelo, Maximiliano A., J. Sebastian Gomez-Cavazos, Arianna Mei, Daniel H. Lackner, and Martin Hetzer. “A Change in Nuclear Pore Complex Composition Regulates Cell Differentiation.” <i>Developmental Cell</i>. Elsevier, 2012. <a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">https://doi.org/10.1016/j.devcel.2011.11.021</a>.","short":"M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental Cell 22 (2012) 446–458.","apa":"D’Angelo, M. A., Gomez-Cavazos, J. S., Mei, A., Lackner, D. H., &#38; Hetzer, M. (2012). A change in nuclear pore complex composition regulates cell differentiation. <i>Developmental Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">https://doi.org/10.1016/j.devcel.2011.11.021</a>"},"publication_status":"published","page":"446-458","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2011.11.021"}],"status":"public","issue":"2","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"month":"01","article_type":"original","oa_version":"Published Version","doi":"10.1016/j.devcel.2011.11.021","quality_controlled":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"extern":"1","abstract":[{"lang":"eng","text":"Nuclear pore complexes (NPCs) are built from ∼30 different proteins called nucleoporins or Nups. Previous studies have shown that several Nups exhibit cell-type-specific expression and that mutations in NPC components result in tissue-specific diseases. Here we show that a specific change in NPC composition is required for both myogenic and neuronal differentiation. The transmembrane nucleoporin Nup210 is absent in proliferating myoblasts and embryonic stem cells (ESCs) but becomes expressed and incorporated into NPCs during cell differentiation. Preventing Nup210 production by RNAi blocks myogenesis and the differentiation of ESCs into neuroprogenitors. We found that the addition of Nup210 to NPCs does not affect nuclear transport but is required for the induction of genes that are essential for cell differentiation. Our results identify a single change in NPC composition as an essential step in cell differentiation and establish a role for Nup210 in gene expression regulation and cell fate determination."}],"external_id":{"pmid":["22264802"]},"publication_identifier":{"issn":["1534-5807"]},"publication":"Developmental Cell","date_created":"2022-04-07T07:52:10Z","year":"2012","date_updated":"2024-10-14T11:26:00Z","_id":"11093","type":"journal_article","intvolume":"        22","article_processing_charge":"No","title":"A change in nuclear pore complex composition regulates cell differentiation","pmid":1,"date_published":"2012-01-19T00:00:00Z","language":[{"iso":"eng"}]}]