[{"extern":"1","volume":161,"external_id":{"pmid":["26091034"]},"year":"2015","citation":{"short":"E.M. Hatch, M. Hetzer, Cell 161 (2015) 1502–1504.","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.","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>","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>","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."},"date_updated":"2022-07-18T08:34:33Z","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."}],"day":"18","doi":"10.1016/j.cell.2015.06.005","quality_controlled":"1","page":"1502-1504","article_type":"original","publisher":"Elsevier","issue":"7","author":[{"full_name":"Hatch, Emily M.","last_name":"Hatch","first_name":"Emily M."},{"first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"scopus_import":"1","pmid":1,"_id":"11073","intvolume":"       161","title":"Linking micronuclei to chromosome fragmentation","article_processing_charge":"No","date_created":"2022-04-07T07:48:49Z","publication_status":"published","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2015.06.005","open_access":"1"}],"type":"journal_article","date_published":"2015-06-18T00:00:00Z","oa":1,"publication_identifier":{"issn":["0092-8674"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"publication":"Cell","month":"06","oa_version":"Published Version"},{"quality_controlled":"1","page":"PR397-R399","publisher":"Elsevier","article_type":"original","scopus_import":"1","pmid":1,"_id":"11074","issue":"10","author":[{"full_name":"Hatch, Emily M.","first_name":"Emily M.","last_name":"Hatch"},{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"date_created":"2022-04-07T07:49:00Z","article_processing_charge":"No","publication_status":"published","intvolume":"        25","title":"Chromothripsis","volume":25,"extern":"1","citation":{"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.","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>","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>","ista":"Hatch EM, Hetzer M. 2015. Chromothripsis. Current Biology. 25(10), PR397-R399.","short":"E.M. Hatch, M. Hetzer, Current Biology 25 (2015) PR397-R399.","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>."},"year":"2015","date_updated":"2022-07-18T08:34:34Z","external_id":{"pmid":["25989073"]},"day":"18","doi":"10.1016/j.cub.2015.02.033","keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"publication":"Current Biology","oa_version":"Published Version","month":"05","main_file_link":[{"url":"https://doi.org/10.1016/j.cub.2015.02.033","open_access":"1"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","type":"journal_article","date_published":"2015-05-18T00:00:00Z","publication_identifier":{"issn":["0960-9822"]},"oa":1},{"citation":{"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>.","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).","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.","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>","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>","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.","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>."},"year":"2015","date_updated":"2021-01-12T08:19:24Z","type":"journal_article","date_published":"2015-10-05T00:00:00Z","publication_identifier":{"issn":["2041-1723"]},"day":"05","doi":"10.1038/ncomms9361","abstract":[{"lang":"eng","text":"The large majority of three-dimensional structures of biological macromolecules have been determined by X-ray diffraction of crystalline samples. High-resolution structure determination crucially depends on the homogeneity of the protein crystal. Overall ‘rocking’ motion of molecules in the crystal is expected to influence diffraction quality, and such motion may therefore affect the process of solving crystal structures. Yet, so far overall molecular motion has not directly been observed in protein crystals, and the timescale of such dynamics remains unclear. Here we use solid-state NMR, X-ray diffraction methods and μs-long molecular dynamics simulations to directly characterize the rigid-body motion of a protein in different crystal forms. For ubiquitin crystals investigated in this study we determine the range of possible correlation times of rocking motion, 0.1–100 μs. The amplitude of rocking varies from one crystal form to another and is correlated with the resolution obtainable in X-ray diffraction experiments."}],"volume":6,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","extern":"1","_id":"8456","publication":"Nature Communications","author":[{"last_name":"Ma","first_name":"Peixiang","full_name":"Ma, Peixiang"},{"last_name":"Xue","first_name":"Yi","full_name":"Xue, Yi"},{"full_name":"Coquelle, Nicolas","first_name":"Nicolas","last_name":"Coquelle"},{"last_name":"Haller","first_name":"Jens D.","full_name":"Haller, Jens D."},{"last_name":"Yuwen","first_name":"Tairan","full_name":"Yuwen, Tairan"},{"full_name":"Ayala, Isabel","first_name":"Isabel","last_name":"Ayala"},{"first_name":"Oleg","last_name":"Mikhailovskii","full_name":"Mikhailovskii, Oleg"},{"last_name":"Willbold","first_name":"Dieter","full_name":"Willbold, Dieter"},{"first_name":"Jacques-Philippe","last_name":"Colletier","full_name":"Colletier, Jacques-Philippe"},{"first_name":"Nikolai R.","last_name":"Skrynnikov","full_name":"Skrynnikov, Nikolai R."},{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"article_processing_charge":"No","date_created":"2020-09-18T10:07:36Z","oa_version":"Published Version","publication_status":"published","article_number":"8361","intvolume":"         6","title":"Observing the overall rocking motion of a protein in a crystal","month":"10","quality_controlled":"1","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"language":[{"iso":"eng"}],"publisher":"Springer Nature","article_type":"original"},{"external_id":{"pmid":["25940229"]},"year":"2015","citation":{"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>","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>","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.","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>.","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).","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>.","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."},"date_updated":"2023-08-22T08:52:56Z","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"}],"day":"05","doi":"10.1038/ncomms8039","extern":"1","volume":6,"author":[{"full_name":"Kraus, P. M.","first_name":"P. M.","last_name":"Kraus"},{"full_name":"Tolstikhin, O. I.","last_name":"Tolstikhin","first_name":"O. I."},{"last_name":"Baykusheva","first_name":"Denitsa Rangelova","full_name":"Baykusheva, Denitsa Rangelova","id":"71b4d059-2a03-11ee-914d-dfa3beed6530"},{"full_name":"Rupenyan, A.","last_name":"Rupenyan","first_name":"A."},{"full_name":"Schneider, J.","first_name":"J.","last_name":"Schneider"},{"full_name":"Bisgaard, C. Z.","first_name":"C. Z.","last_name":"Bisgaard"},{"full_name":"Morishita, T.","last_name":"Morishita","first_name":"T."},{"last_name":"Jensen","first_name":"F.","full_name":"Jensen, F."},{"full_name":"Madsen, L. B.","first_name":"L. B.","last_name":"Madsen"},{"last_name":"Wörner","first_name":"H. J.","full_name":"Wörner, H. J."}],"scopus_import":"1","_id":"14016","pmid":1,"intvolume":"         6","title":"Observation of laser-induced electronic structure in oriented polyatomic molecules","article_processing_charge":"No","date_created":"2023-08-10T06:38:01Z","publication_status":"published","quality_controlled":"1","article_type":"original","publisher":"Springer Nature","type":"journal_article","date_published":"2015-05-05T00:00:00Z","oa":1,"publication_identifier":{"eissn":["2041-1723"]},"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","main_file_link":[{"url":"https://doi.org/10.1038/ncomms8039","open_access":"1"}],"publication":"Nature Communications","article_number":"7039","month":"05","oa_version":"Published Version","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"language":[{"iso":"eng"}]},{"status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2014.02.004","open_access":"1"}],"type":"journal_article","date_published":"2014-02-27T00:00:00Z","oa":1,"publication_identifier":{"issn":["0092-8674"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"publication":"Cell","month":"02","oa_version":"Published Version","extern":"1","volume":156,"external_id":{"pmid":["24581486"]},"citation":{"ista":"Buchwalter A, Hetzer M. 2014. Nuclear pores set the speed limit for mitosis. Cell. 156(5), 868–869.","short":"A. Buchwalter, M. Hetzer, Cell 156 (2014) 868–869.","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>.","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>.","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>","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>"},"year":"2014","date_updated":"2022-07-18T08:44:33Z","abstract":[{"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.","lang":"eng"}],"day":"27","doi":"10.1016/j.cell.2014.02.004","quality_controlled":"1","page":"868-869","article_type":"original","publisher":"Elsevier","issue":"5","author":[{"first_name":"Abigail","last_name":"Buchwalter","full_name":"Buchwalter, Abigail"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W"}],"scopus_import":"1","_id":"11080","pmid":1,"intvolume":"       156","title":"Nuclear pores set the speed limit for mitosis","article_processing_charge":"No","date_created":"2022-04-07T07:50:04Z","publication_status":"published"},{"publication_status":"published","article_processing_charge":"No","date_created":"2023-08-01T09:46:27Z","title":"Nanoporous frameworks exhibiting multiple stimuli responsiveness","intvolume":"         5","_id":"13402","pmid":1,"scopus_import":"1","author":[{"full_name":"Kundu, Pintu K.","first_name":"Pintu K.","last_name":"Kundu"},{"full_name":"Olsen, Gregory L.","first_name":"Gregory L.","last_name":"Olsen"},{"full_name":"Kiss, Vladimir","first_name":"Vladimir","last_name":"Kiss"},{"first_name":"Rafal","last_name":"Klajn","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"publisher":"Springer Nature","article_type":"original","quality_controlled":"1","doi":"10.1038/ncomms4588","day":"07","abstract":[{"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.","lang":"eng"}],"date_updated":"2023-08-08T07:28:10Z","citation":{"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>","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>","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.","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>.","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>.","short":"P.K. Kundu, G.L. Olsen, V. Kiss, R. Klajn, Nature Communications 5 (2014).","ista":"Kundu PK, Olsen GL, Kiss V, Klajn R. 2014. Nanoporous frameworks exhibiting multiple stimuli responsiveness. Nature Communications. 5, 3588."},"year":"2014","external_id":{"pmid":["24709950"]},"volume":5,"extern":"1","oa_version":"Published Version","month":"04","article_number":"3588","publication":"Nature Communications","language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"publication_identifier":{"eissn":["2041-1723"]},"oa":1,"date_published":"2014-04-07T00:00:00Z","type":"journal_article","main_file_link":[{"url":"https://doi.org/10.1038/ncomms4588","open_access":"1"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public"},{"status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2013.06.007"}],"type":"journal_article","date_published":"2013-07-03T00:00:00Z","oa":1,"publication_identifier":{"issn":["0092-8674"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"publication":"Cell","month":"07","oa_version":"Published Version","extern":"1","volume":154,"external_id":{"pmid":["23827674"]},"year":"2013","citation":{"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>.","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.","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>","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>","ista":"Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. 2013. Catastrophic nuclear envelope collapse in cancer cell micronuclei. Cell. 154(1), 47–60.","short":"E.M. Hatch, A.H. Fischer, T.J. Deerinck, M. Hetzer, Cell 154 (2013) 47–60.","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>."},"date_updated":"2022-07-18T08:45:47Z","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."}],"day":"03","doi":"10.1016/j.cell.2013.06.007","quality_controlled":"1","page":"47-60","article_type":"original","publisher":"Elsevier","issue":"1","author":[{"full_name":"Hatch, Emily M.","last_name":"Hatch","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."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"scopus_import":"1","pmid":1,"_id":"11085","intvolume":"       154","title":"Catastrophic nuclear envelope collapse in cancer cell micronuclei","date_created":"2022-04-07T07:50:51Z","article_processing_charge":"No","publication_status":"published"},{"language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"month":"08","oa_version":"Published Version","publication":"Cell","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2013.07.037"}],"oa":1,"publication_identifier":{"issn":["0092-8674"]},"date_published":"2013-08-29T00:00:00Z","type":"journal_article","article_type":"original","publisher":"Elsevier","page":"971-982","quality_controlled":"1","title":"Identification of long-lived proteins reveals exceptional stability of essential cellular structures","intvolume":"       154","publication_status":"published","date_created":"2022-04-07T07:51:08Z","article_processing_charge":"No","author":[{"full_name":"Toyama, Brandon H.","last_name":"Toyama","first_name":"Brandon H."},{"full_name":"Savas, Jeffrey N.","last_name":"Savas","first_name":"Jeffrey N."},{"full_name":"Park, Sung Kyu","first_name":"Sung Kyu","last_name":"Park"},{"full_name":"Harris, Michael S.","first_name":"Michael S.","last_name":"Harris"},{"full_name":"Ingolia, Nicholas T.","first_name":"Nicholas T.","last_name":"Ingolia"},{"last_name":"Yates","first_name":"John R.","full_name":"Yates, John R."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"issue":"5","_id":"11087","pmid":1,"scopus_import":"1","extern":"1","volume":154,"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"}],"doi":"10.1016/j.cell.2013.07.037","day":"29","external_id":{"pmid":["23993091"]},"date_updated":"2022-07-18T08:50:47Z","year":"2013","citation":{"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>.","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.","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>","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.","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>.","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."}},{"main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2012.04.018","open_access":"1"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","date_published":"2012-05-11T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["0092-8674"]},"oa":1,"language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"publication":"Cell","oa_version":"Published Version","month":"05","volume":149,"extern":"1","date_updated":"2022-07-18T08:58:48Z","citation":{"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>","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>","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.","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>.","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>.","short":"E.M. Hatch, M. Hetzer, Cell 149 (2012) 733–735.","ista":"Hatch EM, Hetzer M. 2012. RNP export by nuclear envelope budding. Cell. 149(4), 733–735."},"year":"2012","external_id":{"pmid":["22579277"]},"doi":"10.1016/j.cell.2012.04.018","day":"11","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."}],"page":"733-735","quality_controlled":"1","publisher":"Elsevier","article_type":"letter_note","_id":"11090","pmid":1,"scopus_import":"1","author":[{"first_name":"Emily M.","last_name":"Hatch","full_name":"Hatch, Emily M."},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"issue":"4","publication_status":"published","date_created":"2022-04-07T07:51:45Z","article_processing_charge":"No","title":"RNP export by nuclear envelope budding","intvolume":"       149"},{"article_processing_charge":"No","date_created":"2022-04-07T07:52:10Z","publication_status":"published","intvolume":"        22","title":"A change in nuclear pore complex composition regulates cell differentiation","scopus_import":"1","pmid":1,"_id":"11093","issue":"2","author":[{"first_name":"Maximiliano A.","last_name":"D'Angelo","full_name":"D'Angelo, Maximiliano A."},{"full_name":"Gomez-Cavazos, J. Sebastian","last_name":"Gomez-Cavazos","first_name":"J. Sebastian"},{"first_name":"Arianna","last_name":"Mei","full_name":"Mei, Arianna"},{"full_name":"Lackner, Daniel H.","last_name":"Lackner","first_name":"Daniel H."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"publisher":"Elsevier","article_type":"original","quality_controlled":"1","page":"446-458","day":"19","doi":"10.1016/j.devcel.2011.11.021","abstract":[{"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.","lang":"eng"}],"citation":{"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>.","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.","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>","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>","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.","short":"M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental Cell 22 (2012) 446–458.","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>."},"year":"2012","date_updated":"2022-07-18T08:53:16Z","external_id":{"pmid":["22264802"]},"volume":22,"extern":"1","oa_version":"Published Version","month":"01","publication":"Developmental Cell","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["1534-5807"]},"oa":1,"type":"journal_article","date_published":"2012-01-19T00:00:00Z","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2011.11.021"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public"},{"title":"The nuclear envelope","intvolume":"         2","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:52:49Z","author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"issue":"3","_id":"11097","pmid":1,"scopus_import":"1","article_type":"original","publisher":"Cold Spring Harbor Laboratory","page":"a000539-a000539","quality_controlled":"1","abstract":[{"lang":"eng","text":"The nuclear envelope (NE) is a highly regulated membrane barrier that separates the nucleus from the cytoplasm in eukaryotic cells. It contains a large number of different proteins that have been implicated in chromatin organization and gene regulation. Although the nuclear membrane enables complex levels of gene expression, it also poses a challenge when it comes to cell division. To allow access of the mitotic spindle to chromatin, the nucleus of metazoans must completely disassemble during mitosis, generating the need to re-establish the nuclear compartment at the end of each cell division. Here, I summarize our current understanding of the dynamic remodeling of the NE during the cell cycle."}],"doi":"10.1101/cshperspect.a000539","day":"03","external_id":{"pmid":["20300205"]},"date_updated":"2022-07-18T08:53:50Z","year":"2010","citation":{"short":"M. Hetzer, Cold Spring Harbor Perspectives in Biology 2 (2010) a000539–a000539.","mla":"Hetzer, Martin. “The Nuclear Envelope.” <i>Cold Spring Harbor Perspectives in Biology</i>, vol. 2, no. 3, Cold Spring Harbor Laboratory, 2010, pp. a000539–a000539, doi:<a href=\"https://doi.org/10.1101/cshperspect.a000539\">10.1101/cshperspect.a000539</a>.","ista":"Hetzer M. 2010. The nuclear envelope. Cold Spring Harbor Perspectives in Biology. 2(3), a000539–a000539.","apa":"Hetzer, M. (2010). The nuclear envelope. <i>Cold Spring Harbor Perspectives in Biology</i>. Cold Spring Harbor Laboratory. <a href=\"https://doi.org/10.1101/cshperspect.a000539\">https://doi.org/10.1101/cshperspect.a000539</a>","ama":"Hetzer M. The nuclear envelope. <i>Cold Spring Harbor Perspectives in Biology</i>. 2010;2(3):a000539-a000539. doi:<a href=\"https://doi.org/10.1101/cshperspect.a000539\">10.1101/cshperspect.a000539</a>","chicago":"Hetzer, Martin. “The Nuclear Envelope.” <i>Cold Spring Harbor Perspectives in Biology</i>. Cold Spring Harbor Laboratory, 2010. <a href=\"https://doi.org/10.1101/cshperspect.a000539\">https://doi.org/10.1101/cshperspect.a000539</a>.","ieee":"M. Hetzer, “The nuclear envelope,” <i>Cold Spring Harbor Perspectives in Biology</i>, vol. 2, no. 3. Cold Spring Harbor Laboratory, pp. a000539–a000539, 2010."},"extern":"1","volume":2,"month":"02","oa_version":"None","publication":"Cold Spring Harbor Perspectives in Biology","language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"publication_identifier":{"issn":["1943-0264"]},"date_published":"2010-02-03T00:00:00Z","type":"journal_article","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd"},{"extern":"1","volume":141,"external_id":{"pmid":["20550937"]},"date_updated":"2022-07-18T08:54:52Z","citation":{"ista":"Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041.","short":"C.M. Doucet, J.A. Talamas, M. Hetzer, Cell 141 (2010) 1030–1041.","mla":"Doucet, Christine M., et al. “Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa.” <i>Cell</i>, vol. 141, no. 6, Elsevier, 2010, pp. 1030–41, doi:<a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">10.1016/j.cell.2010.04.036</a>.","chicago":"Doucet, Christine M., Jessica A. Talamas, and Martin Hetzer. “Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa.” <i>Cell</i>. Elsevier, 2010. <a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">https://doi.org/10.1016/j.cell.2010.04.036</a>.","ieee":"C. M. Doucet, J. A. Talamas, and M. Hetzer, “Cell cycle-dependent differences in nuclear pore complex assembly in metazoa,” <i>Cell</i>, vol. 141, no. 6. Elsevier, pp. 1030–1041, 2010.","ama":"Doucet CM, Talamas JA, Hetzer M. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. <i>Cell</i>. 2010;141(6):1030-1041. doi:<a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">10.1016/j.cell.2010.04.036</a>","apa":"Doucet, C. M., Talamas, J. A., &#38; Hetzer, M. (2010). Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">https://doi.org/10.1016/j.cell.2010.04.036</a>"},"year":"2010","abstract":[{"text":"In metazoa, nuclear pore complexes (NPCs) assemble from disassembled precursors into a reforming nuclear envelope (NE) at the end of mitosis and into growing intact NEs during interphase. Here, we show via RNAi-mediated knockdown that ELYS, a nucleoporin critical for the recruitment of the essential Nup107/160 complex to chromatin, is required for NPC assembly at the end of mitosis but not during interphase. Conversely, the transmembrane nucleoporin POM121 is critical for the incorporation of the Nup107/160 complex into new assembly sites specifically during interphase. Strikingly, recruitment of the Nup107/160 complex to an intact NE involves a membrane curvature-sensing domain of its constituent Nup133, which is not required for postmitotic NPC formation. Our results suggest that in organisms with open mitosis, NPCs assemble via two distinct mechanisms to accommodate cell cycle-dependent differences in NE topology.","lang":"eng"}],"doi":"10.1016/j.cell.2010.04.036","day":"11","page":"1030-1041","quality_controlled":"1","article_type":"original","publisher":"Elsevier","author":[{"full_name":"Doucet, Christine M.","last_name":"Doucet","first_name":"Christine M."},{"first_name":"Jessica A.","last_name":"Talamas","full_name":"Talamas, Jessica A."},{"first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"issue":"6","pmid":1,"_id":"11101","scopus_import":"1","title":"Cell cycle-dependent differences in nuclear pore complex assembly in metazoa","intvolume":"       141","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:53:29Z","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2010.04.036","open_access":"1"}],"date_published":"2010-06-11T00:00:00Z","type":"journal_article","oa":1,"publication_identifier":{"issn":["0092-8674"]},"language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"publication":"Cell","month":"06","oa_version":"Published Version"},{"oa":1,"publication_identifier":{"issn":["0092-8674"]},"type":"journal_article","date_published":"2010-02-05T00:00:00Z","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2009.12.054"}],"month":"02","oa_version":"Published Version","publication":"Cell","keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"abstract":[{"text":"Nuclear pore complexes have recently been shown to play roles in gene activation; however their potential involvement in metazoan transcription remains unclear. Here we show that the nucleoporins Sec13, Nup98, and Nup88, as well as a group of FG-repeat nucleoporins, bind to the Drosophila genome at functionally distinct loci that often do not represent nuclear envelope contact sites. Whereas Nup88 localizes to silent loci, Sec13, Nup98, and a subset of FG-repeat nucleoporins bind to developmentally regulated genes undergoing transcription induction. Strikingly, RNAi-mediated knockdown of intranuclear Sec13 and Nup98 specifically inhibits transcription of their target genes and prevents efficient reactivation of transcription after heat shock, suggesting an essential role of NPC components in regulating complex gene expression programs of multicellular organisms.","lang":"eng"}],"day":"05","doi":"10.1016/j.cell.2009.12.054","external_id":{"pmid":["20144761"]},"citation":{"ieee":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, and M. Hetzer, “Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes,” <i>Cell</i>, vol. 140, no. 3. Elsevier, pp. 372–383, 2010.","chicago":"Capelson, Maya, Yun Liang, Roberta Schulte, William Mair, Ulrich Wagner, and Martin Hetzer. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression in Higher Eukaryotes.” <i>Cell</i>. Elsevier, 2010. <a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">https://doi.org/10.1016/j.cell.2009.12.054</a>.","ama":"Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. <i>Cell</i>. 2010;140(3):372-383. doi:<a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">10.1016/j.cell.2009.12.054</a>","apa":"Capelson, M., Liang, Y., Schulte, R., Mair, W., Wagner, U., &#38; Hetzer, M. (2010). Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">https://doi.org/10.1016/j.cell.2009.12.054</a>","ista":"Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. 2010. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell. 140(3), 372–383.","short":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, M. Hetzer, Cell 140 (2010) 372–383.","mla":"Capelson, Maya, et al. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression in Higher Eukaryotes.” <i>Cell</i>, vol. 140, no. 3, Elsevier, 2010, pp. 372–83, doi:<a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">10.1016/j.cell.2009.12.054</a>."},"year":"2010","date_updated":"2022-07-18T08:55:03Z","extern":"1","volume":140,"intvolume":"       140","title":"Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes","article_processing_charge":"No","date_created":"2022-04-07T07:53:36Z","publication_status":"published","issue":"3","author":[{"full_name":"Capelson, Maya","last_name":"Capelson","first_name":"Maya"},{"full_name":"Liang, Yun","first_name":"Yun","last_name":"Liang"},{"last_name":"Schulte","first_name":"Roberta","full_name":"Schulte, Roberta"},{"first_name":"William","last_name":"Mair","full_name":"Mair, William"},{"last_name":"Wagner","first_name":"Ulrich","full_name":"Wagner, Ulrich"},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"scopus_import":"1","pmid":1,"_id":"11102","article_type":"original","publisher":"Elsevier","quality_controlled":"1","page":"372-383"},{"article_type":"review","publisher":"Elsevier","quality_controlled":"1","page":"606-616","intvolume":"        17","title":"Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes","article_processing_charge":"No","date_created":"2022-04-07T07:53:45Z","publication_status":"published","issue":"5","author":[{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"last_name":"Wente","first_name":"Susan R.","full_name":"Wente, Susan R."}],"scopus_import":"1","_id":"11103","pmid":1,"extern":"1","volume":17,"abstract":[{"lang":"eng","text":"Over the last decade, the nuclear envelope (NE) has emerged as a key component in the organization and function of the nuclear genome. As many as 100 different proteins are thought to specifically localize to this double membrane that separates the cytoplasm and the nucleoplasm of eukaryotic cells. Selective portals through the NE are formed at sites where the inner and outer nuclear membranes are fused, and the coincident assembly of ∼30 proteins into nuclear pore complexes occurs. These nuclear pore complexes are essential for the control of nucleocytoplasmic exchange. Many of the NE and nuclear pore proteins are thought to play crucial roles in gene regulation and thus are increasingly linked to human diseases."}],"day":"17","doi":"10.1016/j.devcel.2009.10.007","external_id":{"pmid":["19922866"]},"year":"2009","citation":{"ama":"Hetzer M, Wente SR. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. <i>Developmental Cell</i>. 2009;17(5):606-616. doi:<a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">10.1016/j.devcel.2009.10.007</a>","apa":"Hetzer, M., &#38; Wente, S. R. (2009). Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. <i>Developmental Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">https://doi.org/10.1016/j.devcel.2009.10.007</a>","chicago":"Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis and Organization of the Nuclear Membrane and Pore Complexes.” <i>Developmental Cell</i>. Elsevier, 2009. <a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">https://doi.org/10.1016/j.devcel.2009.10.007</a>.","ieee":"M. Hetzer and S. R. Wente, “Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes,” <i>Developmental Cell</i>, vol. 17, no. 5. Elsevier, pp. 606–616, 2009.","short":"M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.","mla":"Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis and Organization of the Nuclear Membrane and Pore Complexes.” <i>Developmental Cell</i>, vol. 17, no. 5, Elsevier, 2009, pp. 606–16, doi:<a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">10.1016/j.devcel.2009.10.007</a>.","ista":"Hetzer M, Wente SR. 2009. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. Developmental Cell. 17(5), 606–616."},"date_updated":"2022-07-18T08:55:01Z","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"language":[{"iso":"eng"}],"month":"11","oa_version":"Published Version","publication":"Developmental Cell","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2009.10.007"}],"oa":1,"publication_identifier":{"issn":["1534-5807"]},"type":"journal_article","date_published":"2009-11-17T00:00:00Z"},{"oa_version":"Published Version","month":"01","publication":"Cell","language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"publication_identifier":{"issn":["0092-8674"]},"oa":1,"date_published":"2009-01-23T00:00:00Z","type":"journal_article","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2008.11.037"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","publication_status":"published","date_created":"2022-04-07T07:54:52Z","article_processing_charge":"No","title":"Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells","intvolume":"       136","pmid":1,"_id":"11108","scopus_import":"1","author":[{"first_name":"Maximiliano A.","last_name":"D'Angelo","full_name":"D'Angelo, Maximiliano A."},{"full_name":"Raices, Marcela","first_name":"Marcela","last_name":"Raices"},{"full_name":"Panowski, Siler H.","last_name":"Panowski","first_name":"Siler H."},{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"issue":"2","publisher":"Elsevier","article_type":"original","page":"284-295","quality_controlled":"1","doi":"10.1016/j.cell.2008.11.037","day":"23","abstract":[{"lang":"eng","text":"In dividing cells, nuclear pore complexes (NPCs) disassemble during mitosis and reassemble into the newly forming nuclei. However, the fate of nuclear pores in postmitotic cells is unknown. Here, we show that NPCs, unlike other nuclear structures, do not turn over in differentiated cells. While a subset of NPC components, like Nup153 and Nup50, are continuously exchanged, scaffold nucleoporins, like the Nup107/160 complex, are extremely long-lived and remain incorporated in the nuclear membrane during the entire cellular life span. Besides the lack of nucleoporin expression and NPC turnover, we discovered an age-related deterioration of NPCs, leading to an increase in nuclear permeability and the leaking of cytoplasmic proteins into the nucleus. Our finding that nuclear “leakiness” is dramatically accelerated during aging and that a subset of nucleoporins is oxidatively damaged in old cells suggests that the accumulation of damage at the NPC might be a crucial aging event."}],"date_updated":"2022-07-18T08:55:29Z","citation":{"apa":"D’Angelo, M. A., Raices, M., Panowski, S. H., &#38; Hetzer, M. (2009). Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">https://doi.org/10.1016/j.cell.2008.11.037</a>","ama":"D’Angelo MA, Raices M, Panowski SH, Hetzer M. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. <i>Cell</i>. 2009;136(2):284-295. doi:<a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">10.1016/j.cell.2008.11.037</a>","ieee":"M. A. D’Angelo, M. Raices, S. H. Panowski, and M. Hetzer, “Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells,” <i>Cell</i>, vol. 136, no. 2. Elsevier, pp. 284–295, 2009.","chicago":"D’Angelo, Maximiliano A., Marcela Raices, Siler H. Panowski, and Martin Hetzer. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” <i>Cell</i>. Elsevier, 2009. <a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">https://doi.org/10.1016/j.cell.2008.11.037</a>.","mla":"D’Angelo, Maximiliano A., et al. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” <i>Cell</i>, vol. 136, no. 2, Elsevier, 2009, pp. 284–95, doi:<a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">10.1016/j.cell.2008.11.037</a>.","short":"M.A. D’Angelo, M. Raices, S.H. Panowski, M. Hetzer, Cell 136 (2009) 284–295.","ista":"D’Angelo MA, Raices M, Panowski SH, Hetzer M. 2009. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell. 136(2), 284–295."},"year":"2009","external_id":{"pmid":["19167330"]},"volume":136,"extern":"1"},{"volume":113,"extern":"1","day":"17","doi":"10.1016/s0092-8674(03)00235-6","abstract":[{"lang":"eng","text":"Nuclear pore complexes (NPCs) are large multiprotein assemblies that allow traffic between the cytoplasm and the nucleus. During mitosis in higher eukaryotes, the Nuclear Envelope (NE) breaks down and NPCs disassemble. How NPCs reassemble and incorporate into the NE upon mitotic exit is poorly understood. We demonstrate a function for the conserved Nup107-160 complex in this process. Partial in vivo depletion of Nup133 or Nup107 via RNAi in HeLa cells resulted in reduced levels of multiple nucleoporins and decreased NPC density in the NE. Immunodepletion of the entire Nup107-160 complex from in vitro nuclear assembly reactions produced nuclei with a continuous NE but no NPCs. This phenotype was reversible only if Nup107-160 complex was readded before closed NE formation. Depletion also prevented association of FG-repeat nucleoporins with chromatin. We propose a stepwise model in which postmitotic NPC assembly initiates on chromatin via early recruitment of the Nup107-160 complex."}],"year":"2003","citation":{"apa":"Walther, T. C., Alves, A., Pickersgill, H., Loı̈odice, I., Hetzer, M., Galy, V., … Doye, V. (2003). The conserved Nup107-160 complex is critical for nuclear pore complex assembly. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">https://doi.org/10.1016/s0092-8674(03)00235-6</a>","ama":"Walther TC, Alves A, Pickersgill H, et al. The conserved Nup107-160 complex is critical for nuclear pore complex assembly. <i>Cell</i>. 2003;113(2):195-206. doi:<a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">10.1016/s0092-8674(03)00235-6</a>","chicago":"Walther, Tobias C., Annabelle Alves, Helen Pickersgill, Isabelle Loı̈odice, Martin Hetzer, Vincent Galy, Bastian B. Hülsmann, et al. “The Conserved Nup107-160 Complex Is Critical for Nuclear Pore Complex Assembly.” <i>Cell</i>. Elsevier, 2003. <a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">https://doi.org/10.1016/s0092-8674(03)00235-6</a>.","ieee":"T. C. Walther <i>et al.</i>, “The conserved Nup107-160 complex is critical for nuclear pore complex assembly,” <i>Cell</i>, vol. 113, no. 2. Elsevier, pp. 195–206, 2003.","short":"T.C. Walther, A. Alves, H. Pickersgill, I. Loı̈odice, M. Hetzer, V. Galy, B.B. Hülsmann, T. Köcher, M. Wilm, T. Allen, I.W. Mattaj, V. Doye, Cell 113 (2003) 195–206.","mla":"Walther, Tobias C., et al. “The Conserved Nup107-160 Complex Is Critical for Nuclear Pore Complex Assembly.” <i>Cell</i>, vol. 113, no. 2, Elsevier, 2003, pp. 195–206, doi:<a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">10.1016/s0092-8674(03)00235-6</a>.","ista":"Walther TC, Alves A, Pickersgill H, Loı̈odice I, Hetzer M, Galy V, Hülsmann BB, Köcher T, Wilm M, Allen T, Mattaj IW, Doye V. 2003. The conserved Nup107-160 complex is critical for nuclear pore complex assembly. Cell. 113(2), 195–206."},"date_updated":"2022-07-18T08:57:42Z","external_id":{"pmid":["12705868"]},"publisher":"Elsevier","article_type":"original","quality_controlled":"1","page":"195-206","article_processing_charge":"No","date_created":"2022-04-07T07:57:10Z","publication_status":"published","intvolume":"       113","title":"The conserved Nup107-160 complex is critical for nuclear pore complex assembly","scopus_import":"1","pmid":1,"_id":"11122","issue":"2","author":[{"last_name":"Walther","first_name":"Tobias C.","full_name":"Walther, Tobias C."},{"first_name":"Annabelle","last_name":"Alves","full_name":"Alves, Annabelle"},{"first_name":"Helen","last_name":"Pickersgill","full_name":"Pickersgill, Helen"},{"first_name":"Isabelle","last_name":"Loı̈odice","full_name":"Loı̈odice, Isabelle"},{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"full_name":"Galy, Vincent","first_name":"Vincent","last_name":"Galy"},{"first_name":"Bastian B.","last_name":"Hülsmann","full_name":"Hülsmann, Bastian B."},{"last_name":"Köcher","first_name":"Thomas","full_name":"Köcher, Thomas"},{"full_name":"Wilm, Matthias","first_name":"Matthias","last_name":"Wilm"},{"full_name":"Allen, Terry","last_name":"Allen","first_name":"Terry"},{"first_name":"Iain W.","last_name":"Mattaj","full_name":"Mattaj, Iain W."},{"full_name":"Doye, Valérie","first_name":"Valérie","last_name":"Doye"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","publication_identifier":{"issn":["0092-8674"]},"type":"journal_article","date_published":"2003-04-17T00:00:00Z","keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"oa_version":"Published Version","month":"04","publication":"Cell"},{"article_type":"letter_note","publisher":"Elsevier BV","quality_controlled":"1","page":"1151-1156","intvolume":"        12","title":"Ran binds to chromatin by two distinct mechanisms","date_created":"2022-04-07T07:57:31Z","article_processing_charge":"No","publication_status":"published","issue":"13","author":[{"full_name":"Bilbao-Cortés, Daniel","last_name":"Bilbao-Cortés","first_name":"Daniel"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"},{"last_name":"Längst","first_name":"Gernot","full_name":"Längst, Gernot"},{"full_name":"Becker, Peter B.","last_name":"Becker","first_name":"Peter B."},{"full_name":"Mattaj, Iain W.","first_name":"Iain W.","last_name":"Mattaj"}],"scopus_import":"1","pmid":1,"_id":"11124","extern":"1","volume":12,"abstract":[{"lang":"eng","text":"Ran GTPase plays important roles in nucleocytoplasmic transport in interphase [1, 2] and in both spindle formation and nuclear envelope (NE) assembly during mitosis [3, 4, 5]. The latter functions rely on the presence of high local concentrations of GTP-bound Ran near mitotic chromatin [3, 4, 5]. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin [6, 7, 8, 9], but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes. We propose that the Ran binding capacity of chromatin contributes to localized spindle and NE assembly."}],"day":"09","doi":"10.1016/s0960-9822(02)00927-2","external_id":{"pmid":["12121625"]},"year":"2002","citation":{"chicago":"Bilbao-Cortés, Daniel, Martin Hetzer, Gernot Längst, Peter B. Becker, and Iain W. Mattaj. “Ran Binds to Chromatin by Two Distinct Mechanisms.” <i>Current Biology</i>. Elsevier BV, 2002. <a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">https://doi.org/10.1016/s0960-9822(02)00927-2</a>.","ieee":"D. Bilbao-Cortés, M. Hetzer, G. Längst, P. B. Becker, and I. W. Mattaj, “Ran binds to chromatin by two distinct mechanisms,” <i>Current Biology</i>, vol. 12, no. 13. Elsevier BV, pp. 1151–1156, 2002.","ama":"Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. Ran binds to chromatin by two distinct mechanisms. <i>Current Biology</i>. 2002;12(13):1151-1156. doi:<a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">10.1016/s0960-9822(02)00927-2</a>","apa":"Bilbao-Cortés, D., Hetzer, M., Längst, G., Becker, P. B., &#38; Mattaj, I. W. (2002). Ran binds to chromatin by two distinct mechanisms. <i>Current Biology</i>. Elsevier BV. <a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">https://doi.org/10.1016/s0960-9822(02)00927-2</a>","ista":"Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. 2002. Ran binds to chromatin by two distinct mechanisms. Current Biology. 12(13), 1151–1156.","mla":"Bilbao-Cortés, Daniel, et al. “Ran Binds to Chromatin by Two Distinct Mechanisms.” <i>Current Biology</i>, vol. 12, no. 13, Elsevier BV, 2002, pp. 1151–56, doi:<a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">10.1016/s0960-9822(02)00927-2</a>.","short":"D. Bilbao-Cortés, M. Hetzer, G. Längst, P.B. Becker, I.W. Mattaj, Current Biology 12 (2002) 1151–1156."},"date_updated":"2022-07-18T08:58:05Z","keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"month":"07","oa_version":"Published Version","publication":"Current Biology","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"url":"https://doi.org/10.1016/S0960-9822(02)00927-2","open_access":"1"}],"oa":1,"publication_identifier":{"issn":["0960-9822"]},"type":"journal_article","date_published":"2002-07-09T00:00:00Z"}]