[{"type":"journal_article","article_processing_charge":"No","citation":{"ama":"Mertens J, Paquola ACM, Ku M, et al. Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects. <i>Cell Stem Cell</i>. 2015;17(6):705-718. doi:<a href=\"https://doi.org/10.1016/j.stem.2015.09.001\">10.1016/j.stem.2015.09.001</a>","ista":"Mertens J, Paquola ACM, Ku M, Hatch E, Böhnke L, Ladjevardi S, McGrath S, Campbell B, Lee H, Herdy JR, Gonçalves JT, Toda T, Kim Y, Winkler J, Yao J, Hetzer M, Gage FH. 2015. Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects. Cell Stem Cell. 17(6), 705–718.","short":"J. Mertens, A.C.M. Paquola, M. Ku, E. Hatch, L. Böhnke, S. Ladjevardi, S. McGrath, B. Campbell, H. Lee, J.R. Herdy, J.T. Gonçalves, T. Toda, Y. Kim, J. Winkler, J. Yao, M. Hetzer, F.H. Gage, Cell Stem Cell 17 (2015) 705–718.","mla":"Mertens, Jerome, et al. “Directly Reprogrammed Human Neurons Retain Aging-Associated Transcriptomic Signatures and Reveal Age-Related Nucleocytoplasmic Defects.” <i>Cell Stem Cell</i>, vol. 17, no. 6, Elsevier, 2015, pp. 705–18, doi:<a href=\"https://doi.org/10.1016/j.stem.2015.09.001\">10.1016/j.stem.2015.09.001</a>.","chicago":"Mertens, Jerome, Apuã C.M. Paquola, Manching Ku, Emily Hatch, Lena Böhnke, Shauheen Ladjevardi, Sean McGrath, et al. “Directly Reprogrammed Human Neurons Retain Aging-Associated Transcriptomic Signatures and Reveal Age-Related Nucleocytoplasmic Defects.” <i>Cell Stem Cell</i>. Elsevier, 2015. <a href=\"https://doi.org/10.1016/j.stem.2015.09.001\">https://doi.org/10.1016/j.stem.2015.09.001</a>.","ieee":"J. Mertens <i>et al.</i>, “Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects,” <i>Cell Stem Cell</i>, vol. 17, no. 6. Elsevier, pp. 705–718, 2015.","apa":"Mertens, J., Paquola, A. C. M., Ku, M., Hatch, E., Böhnke, L., Ladjevardi, S., … Gage, F. H. (2015). Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects. <i>Cell Stem Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.stem.2015.09.001\">https://doi.org/10.1016/j.stem.2015.09.001</a>"},"publisher":"Elsevier","date_updated":"2022-07-18T08:44:21Z","oa_version":"Published Version","status":"public","month":"12","scopus_import":"1","date_created":"2022-04-07T07:49:51Z","external_id":{"pmid":["26456686"]},"publication_status":"published","abstract":[{"text":"Aging is a major risk factor for many human diseases, and in vitro generation of human neurons is an attractive approach for modeling aging-related brain disorders. However, modeling aging in differentiated human neurons has proved challenging. We generated neurons from human donors across a broad range of ages, either by iPSC-based reprogramming and differentiation or by direct conversion into induced neurons (iNs). While iPSCs and derived neurons did not retain aging-associated gene signatures, iNs displayed age-specific transcriptional profiles and revealed age-associated decreases in the nuclear transport receptor RanBP17. We detected an age-dependent loss of nucleocytoplasmic compartmentalization (NCC) in donor fibroblasts and corresponding iNs and found that reduced RanBP17 impaired NCC in young cells, while iPSC rejuvenation restored NCC in aged cells. These results show that iNs retain important aging-related signatures, thus allowing modeling of the aging process in vitro, and they identify impaired NCC as an important factor in human aging.","lang":"eng"}],"issue":"6","quality_controlled":"1","_id":"11079","intvolume":"        17","date_published":"2015-12-03T00:00:00Z","author":[{"last_name":"Mertens","full_name":"Mertens, Jerome","first_name":"Jerome"},{"first_name":"Apuã C.M.","full_name":"Paquola, Apuã C.M.","last_name":"Paquola"},{"last_name":"Ku","first_name":"Manching","full_name":"Ku, Manching"},{"full_name":"Hatch, Emily","first_name":"Emily","last_name":"Hatch"},{"last_name":"Böhnke","full_name":"Böhnke, Lena","first_name":"Lena"},{"last_name":"Ladjevardi","full_name":"Ladjevardi, Shauheen","first_name":"Shauheen"},{"last_name":"McGrath","first_name":"Sean","full_name":"McGrath, Sean"},{"full_name":"Campbell, Benjamin","first_name":"Benjamin","last_name":"Campbell"},{"first_name":"Hyungjun","full_name":"Lee, Hyungjun","last_name":"Lee"},{"last_name":"Herdy","first_name":"Joseph R.","full_name":"Herdy, Joseph R."},{"last_name":"Gonçalves","full_name":"Gonçalves, J. Tiago","first_name":"J. Tiago"},{"last_name":"Toda","full_name":"Toda, Tomohisa","first_name":"Tomohisa"},{"last_name":"Kim","full_name":"Kim, Yongsung","first_name":"Yongsung"},{"full_name":"Winkler, Jürgen","first_name":"Jürgen","last_name":"Winkler"},{"first_name":"Jun","full_name":"Yao, Jun","last_name":"Yao"},{"full_name":"HETZER, Martin W","first_name":"Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"},{"last_name":"Gage","full_name":"Gage, Fred H.","first_name":"Fred H."}],"volume":17,"page":"705-718","article_type":"original","keyword":["Cell Biology","Genetics","Molecular Medicine"],"oa":1,"language":[{"iso":"eng"}],"publication_identifier":{"issn":["1934-5909"]},"doi":"10.1016/j.stem.2015.09.001","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication":"Cell Stem Cell","day":"03","main_file_link":[{"url":"https://doi.org/10.1016/j.stem.2015.09.001","open_access":"1"}],"title":"Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects","year":"2015","extern":"1","pmid":1},{"article_type":"original","keyword":["Statistics and Probability","Computational Theory and Mathematics","Biochemistry","Molecular Biology","Computational Mathematics","Computer Science Applications"],"publication_identifier":{"issn":["1367-4803","1460-2059"]},"language":[{"iso":"eng"}],"doi":"10.1093/bioinformatics/btu166","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Bioinformatics","day":"01","title":"Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data","year":"2014","extern":"1","type":"journal_article","article_processing_charge":"No","citation":{"chicago":"Morin, Sébastien, Troels E Linnet, Mathilde Lescanne, Paul Schanda, Gary S Thompson, Martin Tollinger, Kaare Teilum, et al. “Relax: The Analysis of Biomolecular Kinetics and Thermodynamics Using NMR Relaxation Dispersion Data.” <i>Bioinformatics</i>. Oxford University Press, 2014. <a href=\"https://doi.org/10.1093/bioinformatics/btu166\">https://doi.org/10.1093/bioinformatics/btu166</a>.","apa":"Morin, S., Linnet, T. E., Lescanne, M., Schanda, P., Thompson, G. S., Tollinger, M., … d’Auvergne, E. J. (2014). Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. <i>Bioinformatics</i>. Oxford University Press. <a href=\"https://doi.org/10.1093/bioinformatics/btu166\">https://doi.org/10.1093/bioinformatics/btu166</a>","ieee":"S. Morin <i>et al.</i>, “Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data,” <i>Bioinformatics</i>, vol. 30, no. 15. Oxford University Press, pp. 2219–2220, 2014.","ista":"Morin S, Linnet TE, Lescanne M, Schanda P, Thompson GS, Tollinger M, Teilum K, Gagné S, Marion D, Griesinger C, Blackledge M, d’Auvergne EJ. 2014. Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. Bioinformatics. 30(15), 2219–2220.","ama":"Morin S, Linnet TE, Lescanne M, et al. Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. <i>Bioinformatics</i>. 2014;30(15):2219-2220. doi:<a href=\"https://doi.org/10.1093/bioinformatics/btu166\">10.1093/bioinformatics/btu166</a>","mla":"Morin, Sébastien, et al. “Relax: The Analysis of Biomolecular Kinetics and Thermodynamics Using NMR Relaxation Dispersion Data.” <i>Bioinformatics</i>, vol. 30, no. 15, Oxford University Press, 2014, pp. 2219–20, doi:<a href=\"https://doi.org/10.1093/bioinformatics/btu166\">10.1093/bioinformatics/btu166</a>.","short":"S. Morin, T.E. Linnet, M. Lescanne, P. Schanda, G.S. Thompson, M. Tollinger, K. Teilum, S. Gagné, D. Marion, C. Griesinger, M. Blackledge, E.J. d’Auvergne, Bioinformatics 30 (2014) 2219–2220."},"publisher":"Oxford University Press","date_updated":"2021-01-12T08:19:25Z","oa_version":"None","status":"public","month":"08","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1093/bioinformatics/btz397"}]},"publication_status":"published","date_created":"2020-09-18T10:08:07Z","abstract":[{"text":"Nuclear magnetic resonance (NMR) is a powerful tool for observing the motion of biomolecules at the atomic level. One technique, the analysis of relaxation dispersion phenomenon, is highly suited for studying the kinetics and thermodynamics of biological processes. Built on top of the relax computational environment for NMR dynamics is a new dispersion analysis designed to be comprehensive, accurate and easy-to-use. The software supports more models, both numeric and analytic, than current solutions. An automated protocol, available for scripting and driving the graphical user interface (GUI), is designed to simplify the analysis of dispersion data for NMR spectroscopists. Decreases in optimization time are granted by parallelization for running on computer clusters and by skipping an initial grid search by using parameters from one solution as the starting point for another —using analytic model results for the numeric models, taking advantage of model nesting, and using averaged non-clustered results for the clustered analysis.","lang":"eng"}],"issue":"15","quality_controlled":"1","_id":"8459","date_published":"2014-08-01T00:00:00Z","intvolume":"        30","page":"2219-2220","volume":30,"author":[{"last_name":"Morin","first_name":"Sébastien","full_name":"Morin, Sébastien"},{"last_name":"Linnet","full_name":"Linnet, Troels E","first_name":"Troels E"},{"last_name":"Lescanne","first_name":"Mathilde","full_name":"Lescanne, Mathilde"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda"},{"first_name":"Gary S","full_name":"Thompson, Gary S","last_name":"Thompson"},{"full_name":"Tollinger, Martin","first_name":"Martin","last_name":"Tollinger"},{"full_name":"Teilum, Kaare","first_name":"Kaare","last_name":"Teilum"},{"last_name":"Gagné","first_name":"Stéphane","full_name":"Gagné, Stéphane"},{"last_name":"Marion","full_name":"Marion, Dominique","first_name":"Dominique"},{"first_name":"Christian","full_name":"Griesinger, Christian","last_name":"Griesinger"},{"first_name":"Martin","full_name":"Blackledge, Martin","last_name":"Blackledge"},{"last_name":"d’Auvergne","full_name":"d’Auvergne, Edward J","first_name":"Edward J"}]},{"title":"Nanoporous frameworks exhibiting multiple stimuli responsiveness","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms4588"}],"pmid":1,"extern":"1","year":"2014","language":[{"iso":"eng"}],"publication_identifier":{"eissn":["2041-1723"]},"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"oa":1,"article_type":"original","article_number":"3588","publication":"Nature Communications","day":"07","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","doi":"10.1038/ncomms4588","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."}],"publication_status":"published","external_id":{"pmid":["24709950"]},"date_created":"2023-08-01T09:46:27Z","scopus_import":"1","date_published":"2014-04-07T00:00:00Z","intvolume":"         5","author":[{"first_name":"Pintu K.","full_name":"Kundu, Pintu K.","last_name":"Kundu"},{"last_name":"Olsen","full_name":"Olsen, Gregory L.","first_name":"Gregory L."},{"first_name":"Vladimir","full_name":"Kiss, Vladimir","last_name":"Kiss"},{"id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","full_name":"Klajn, Rafal","first_name":"Rafal","last_name":"Klajn"}],"volume":5,"_id":"13402","quality_controlled":"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>","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).","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>","ista":"Kundu PK, Olsen GL, Kiss V, Klajn R. 2014. Nanoporous frameworks exhibiting multiple stimuli responsiveness. Nature Communications. 5, 3588."},"publisher":"Springer Nature","article_processing_charge":"No","type":"journal_article","status":"public","month":"04","date_updated":"2023-08-08T07:28:10Z","oa_version":"Published Version"},{"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1111/cga.12039"}],"title":"Molecular and cellular mechanisms of development underlying congenital diseases","department":[{"_id":"CaHe"}],"year":"2014","acknowledgement":"The authors thank all the members of the Division of Morphogenesis, National Institute for Basic Biology, for their contributions to the research, their encouragement, and helpful discussions, particularly Dr M. Suzuki for his critical reading of the manuscript. We also thank the Model Animal Research and Spectrography and Bioimaging Facilities, NIBB Core Research Facilities, for technical support. M.H. was supported by a research fellowship from the Japan Society for the Promotion of Science (JSPS). Our work introduced in this review was supported by a Grant-in-Aid for Scientific Research on Innovative Areas from the Ministry of Education, Culture, Sports, Science, and Technology (MEXT), Japan, to N.U.","pmid":1,"article_type":"original","publication_identifier":{"issn":["0914-3505"]},"language":[{"iso":"eng"}],"keyword":["Developmental Biology","Embryology","General Medicine","Pediatrics","Perinatology","and Child Health"],"oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","doi":"10.1111/cga.12039","day":"01","publication":"Congenital Anomalies","scopus_import":"1","abstract":[{"text":"In the last several decades, developmental biology has clarified the molecular mechanisms of embryogenesis and organogenesis. In particular, it has demonstrated that the “tool-kit genes” essential for regulating developmental processes are not only highly conserved among species, but are also used as systems at various times and places in an organism to control distinct developmental events. Therefore, mutations in many of these tool-kit genes may cause congenital diseases involving morphological abnormalities. This link between genes and abnormal morphological phenotypes underscores the importance of understanding how cells behave and contribute to morphogenesis as a result of gene function. Recent improvements in live imaging and in quantitative analyses of cellular dynamics will advance our understanding of the cellular pathogenesis of congenital diseases associated with aberrant morphologies. In these studies, it is critical to select an appropriate model organism for the particular phenomenon of interest.","lang":"eng"}],"external_id":{"pmid":["24666178"]},"date_created":"2022-03-04T08:17:25Z","publication_status":"published","_id":"10815","quality_controlled":"1","issue":"1","page":"1-7","volume":54,"author":[{"last_name":"Hashimoto","first_name":"Masakazu","full_name":"Hashimoto, Masakazu"},{"first_name":"Hitoshi","id":"4C6E54C6-F248-11E8-B48F-1D18A9856A87","full_name":"Morita, Hitoshi","last_name":"Morita"},{"last_name":"Ueno","first_name":"Naoto","full_name":"Ueno, Naoto"}],"date_published":"2014-02-01T00:00:00Z","intvolume":"        54","type":"journal_article","publisher":"Wiley","citation":{"ieee":"M. Hashimoto, H. Morita, and N. Ueno, “Molecular and cellular mechanisms of development underlying congenital diseases,” <i>Congenital Anomalies</i>, vol. 54, no. 1. Wiley, pp. 1–7, 2014.","apa":"Hashimoto, M., Morita, H., &#38; Ueno, N. (2014). Molecular and cellular mechanisms of development underlying congenital diseases. <i>Congenital Anomalies</i>. Wiley. <a href=\"https://doi.org/10.1111/cga.12039\">https://doi.org/10.1111/cga.12039</a>","chicago":"Hashimoto, Masakazu, Hitoshi Morita, and Naoto Ueno. “Molecular and Cellular Mechanisms of Development Underlying Congenital Diseases.” <i>Congenital Anomalies</i>. Wiley, 2014. <a href=\"https://doi.org/10.1111/cga.12039\">https://doi.org/10.1111/cga.12039</a>.","short":"M. Hashimoto, H. Morita, N. Ueno, Congenital Anomalies 54 (2014) 1–7.","mla":"Hashimoto, Masakazu, et al. “Molecular and Cellular Mechanisms of Development Underlying Congenital Diseases.” <i>Congenital Anomalies</i>, vol. 54, no. 1, Wiley, 2014, pp. 1–7, doi:<a href=\"https://doi.org/10.1111/cga.12039\">10.1111/cga.12039</a>.","ama":"Hashimoto M, Morita H, Ueno N. Molecular and cellular mechanisms of development underlying congenital diseases. <i>Congenital Anomalies</i>. 2014;54(1):1-7. doi:<a href=\"https://doi.org/10.1111/cga.12039\">10.1111/cga.12039</a>","ista":"Hashimoto M, Morita H, Ueno N. 2014. Molecular and cellular mechanisms of development underlying congenital diseases. Congenital Anomalies. 54(1), 1–7."},"article_processing_charge":"No","month":"02","status":"public","oa_version":"None","date_updated":"2022-03-04T08:26:05Z"},{"year":"2014","pmid":1,"extern":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2014.02.004"}],"title":"Nuclear pores set the speed limit for mitosis","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","doi":"10.1016/j.cell.2014.02.004","day":"27","publication":"Cell","article_type":"original","language":[{"iso":"eng"}],"publication_identifier":{"issn":["0092-8674"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"oa":1,"_id":"11080","quality_controlled":"1","issue":"5","author":[{"full_name":"Buchwalter, Abigail","first_name":"Abigail","last_name":"Buchwalter"},{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"}],"page":"868-869","volume":156,"intvolume":"       156","date_published":"2014-02-27T00:00:00Z","scopus_import":"1","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."}],"external_id":{"pmid":["24581486"]},"date_created":"2022-04-07T07:50:04Z","publication_status":"published","month":"02","status":"public","oa_version":"Published Version","date_updated":"2022-07-18T08:44:33Z","type":"journal_article","publisher":"Elsevier","citation":{"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>","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>","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>.","short":"A. Buchwalter, M. Hetzer, Cell 156 (2014) 868–869."},"article_processing_charge":"No"},{"day":"21","publication":"Journal of Cell Biology","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","doi":"10.1083/jcb.201402003","language":[{"iso":"eng"}],"publication_identifier":{"issn":["1540-8140","0021-9525"]},"oa":1,"keyword":["Cell Biology"],"article_type":"review","pmid":1,"extern":"1","year":"2014","title":"Breaching the nuclear envelope in development and disease","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.201402003"}],"month":"04","status":"public","oa_version":"Published Version","date_updated":"2022-07-18T08:45:09Z","publisher":"Rockefeller University Press","citation":{"ista":"Hatch E, Hetzer M. 2014. Breaching the nuclear envelope in development and disease. Journal of Cell Biology. 205(2), 133–141.","ama":"Hatch E, Hetzer M. Breaching the nuclear envelope in development and disease. <i>Journal of Cell Biology</i>. 2014;205(2):133-141. doi:<a href=\"https://doi.org/10.1083/jcb.201402003\">10.1083/jcb.201402003</a>","short":"E. Hatch, M. Hetzer, Journal of Cell Biology 205 (2014) 133–141.","mla":"Hatch, Emily, and Martin Hetzer. “Breaching the Nuclear Envelope in Development and Disease.” <i>Journal of Cell Biology</i>, vol. 205, no. 2, Rockefeller University Press, 2014, pp. 133–41, doi:<a href=\"https://doi.org/10.1083/jcb.201402003\">10.1083/jcb.201402003</a>.","chicago":"Hatch, Emily, and Martin Hetzer. “Breaching the Nuclear Envelope in Development and Disease.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2014. <a href=\"https://doi.org/10.1083/jcb.201402003\">https://doi.org/10.1083/jcb.201402003</a>.","ieee":"E. Hatch and M. Hetzer, “Breaching the nuclear envelope in development and disease,” <i>Journal of Cell Biology</i>, vol. 205, no. 2. Rockefeller University Press, pp. 133–141, 2014.","apa":"Hatch, E., &#38; Hetzer, M. (2014). Breaching the nuclear envelope in development and disease. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201402003\">https://doi.org/10.1083/jcb.201402003</a>"},"article_processing_charge":"No","type":"journal_article","page":"133-141","author":[{"last_name":"Hatch","first_name":"Emily","full_name":"Hatch, Emily"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"volume":205,"intvolume":"       205","date_published":"2014-04-21T00:00:00Z","_id":"11081","issue":"2","quality_controlled":"1","abstract":[{"lang":"eng","text":"In eukaryotic cells the nuclear genome is enclosed by the nuclear envelope (NE). In metazoans, the NE breaks down in mitosis and it has been assumed that the physical barrier separating nucleoplasm and cytoplasm remains intact during the rest of the cell cycle and cell differentiation. However, recent studies suggest that nonmitotic NE remodeling plays a critical role in development, virus infection, laminopathies, and cancer. Although the mechanisms underlying these NE restructuring events are currently being defined, one common theme is activation of protein kinase C family members in the interphase nucleus to disrupt the nuclear lamina, demonstrating the importance of the lamina in maintaining nuclear integrity."}],"external_id":{"pmid":["24751535"]},"date_created":"2022-04-07T07:50:13Z","publication_status":"published","scopus_import":"1"},{"title":"Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1091/mbc.e14-04-0865"}],"extern":"1","year":"2014","publication_identifier":{"issn":["1059-1524","1939-4586"]},"language":[{"iso":"eng"}],"oa":1,"keyword":["Cell Biology","Molecular Biology"],"article_type":"original","publication":"Molecular Biology of the Cell","day":"15","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","doi":"10.1091/mbc.e14-04-0865","abstract":[{"lang":"eng","text":"The nuclear pore complex (NPC) plays a critical role in gene expression by mediating import of transcription regulators into the nucleus and export of RNA transcripts to the cytoplasm. Emerging evidence suggests that in addition to mediating transport, a subset of nucleoporins (Nups) engage in transcriptional activation and elongation at genomic loci that are not associated with NPCs. The underlying mechanism and regulation of Nup mobility on and off nuclear pores remain unclear. Here we show that Nup50 is a mobile Nup with a pronounced presence both at the NPC and in the nucleoplasm that can move between these different localizations. Strikingly, the dynamic behavior of Nup50 in both locations is dependent on active transcription by RNA polymerase II and requires the N-terminal half of the protein, which contains importin α– and Nup153-binding domains. However, Nup50 dynamics are independent of importin α, Nup153, and Nup98, even though the latter two proteins also exhibit transcription-dependent mobility. Of interest, depletion of Nup50 from C2C12 myoblasts does not affect cell proliferation but inhibits differentiation into myotubes. Taken together, our results suggest a transport-independent role for Nup50 in chromatin biology that occurs away from the NPC."}],"publication_status":"published","date_created":"2022-04-07T07:50:24Z","scopus_import":"1","date_published":"2014-08-15T00:00:00Z","intvolume":"        25","page":"2472-2484","volume":25,"author":[{"last_name":"Buchwalter","full_name":"Buchwalter, Abigail L.","first_name":"Abigail L."},{"last_name":"Liang","first_name":"Yun","full_name":"Liang, Yun"},{"first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"_id":"11082","quality_controlled":"1","issue":"16","citation":{"chicago":"Buchwalter, Abigail L., Yun Liang, and Martin Hetzer. “Nup50 Is Required for Cell Differentiation and Exhibits Transcription-Dependent Dynamics.” <i>Molecular Biology of the Cell</i>. American Society for Cell Biology, 2014. <a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">https://doi.org/10.1091/mbc.e14-04-0865</a>.","apa":"Buchwalter, A. L., Liang, Y., &#38; Hetzer, M. (2014). Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics. <i>Molecular Biology of the Cell</i>. American Society for Cell Biology. <a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">https://doi.org/10.1091/mbc.e14-04-0865</a>","ieee":"A. L. Buchwalter, Y. Liang, and M. Hetzer, “Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics,” <i>Molecular Biology of the Cell</i>, vol. 25, no. 16. American Society for Cell Biology, pp. 2472–2484, 2014.","ista":"Buchwalter AL, Liang Y, Hetzer M. 2014. Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics. Molecular Biology of the Cell. 25(16), 2472–2484.","ama":"Buchwalter AL, Liang Y, Hetzer M. Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics. <i>Molecular Biology of the Cell</i>. 2014;25(16):2472-2484. doi:<a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">10.1091/mbc.e14-04-0865</a>","short":"A.L. Buchwalter, Y. Liang, M. Hetzer, Molecular Biology of the Cell 25 (2014) 2472–2484.","mla":"Buchwalter, Abigail L., et al. “Nup50 Is Required for Cell Differentiation and Exhibits Transcription-Dependent Dynamics.” <i>Molecular Biology of the Cell</i>, vol. 25, no. 16, American Society for Cell Biology, 2014, pp. 2472–84, doi:<a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">10.1091/mbc.e14-04-0865</a>."},"publisher":"American Society for Cell Biology","article_processing_charge":"No","type":"journal_article","month":"08","status":"public","date_updated":"2022-07-18T08:45:20Z","oa_version":"Published Version"},{"abstract":[{"lang":"eng","text":"The transition of proteins from their soluble functional state to amyloid fibrils and aggregates is associated with the onset of several human diseases. Protein aggregation often requires some structural reshaping and the subsequent formation of intermolecular contacts. Therefore, the study of the conformation of excited protein states and their ability to form oligomers is of primary importance for understanding the molecular basis of amyloid fibril formation. Here, we investigated the oligomerization processes that occur along the folding of the amyloidogenic human protein β2-microglobulin. The combination of real-time two-dimensional NMR data with real-time small-angle X-ray scattering measurements allowed us to derive thermodynamic and kinetic information on protein oligomerization of different conformational states populated along the folding pathways. In particular, we could demonstrate that a long-lived folding intermediate (I-state) has a higher propensity to oligomerize compared to the native state. Our data agree well with a simple five-state kinetic model that involves only monomeric and dimeric species. The dimers have an elongated shape with the dimerization interface located at the apical side of β2-microglobulin close to Pro32, the residue that has a trans conformation in the I-state and a cis conformation in the native (N) state. Our experimental data suggest that partial unfolding in the apical half of the protein close to Pro32 leads to an excited state conformation with enhanced propensity for oligomerization. This excited state becomes more populated in the transient I-state due to the destabilization of the native conformation by the trans-Pro32 configuration."}],"title":"Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure","publication_status":"published","date_created":"2020-09-18T10:09:12Z","_id":"8462","year":"2013","issue":"15","quality_controlled":"1","intvolume":"       425","extern":"1","date_published":"2013-08-09T00:00:00Z","author":[{"last_name":"Rennella","full_name":"Rennella, E.","first_name":"E."},{"last_name":"Cutuil","first_name":"T.","full_name":"Cutuil, T."},{"last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"first_name":"I.","full_name":"Ayala, I.","last_name":"Ayala"},{"last_name":"Gabel","full_name":"Gabel, F.","first_name":"F."},{"full_name":"Forge, V.","first_name":"V.","last_name":"Forge"},{"last_name":"Corazza","full_name":"Corazza, A.","first_name":"A."},{"full_name":"Esposito, G.","first_name":"G.","last_name":"Esposito"},{"last_name":"Brutscher","first_name":"B.","full_name":"Brutscher, B."}],"volume":425,"page":"2722-2736","article_type":"original","type":"journal_article","citation":{"mla":"Rennella, E., et al. “Oligomeric States along the Folding Pathways of Β2-Microglobulin: Kinetics, Thermodynamics, and Structure.” <i>Journal of Molecular Biology</i>, vol. 425, no. 15, Elsevier, 2013, pp. 2722–36, doi:<a href=\"https://doi.org/10.1016/j.jmb.2013.04.028\">10.1016/j.jmb.2013.04.028</a>.","short":"E. Rennella, T. Cutuil, P. Schanda, I. Ayala, F. Gabel, V. Forge, A. Corazza, G. Esposito, B. Brutscher, Journal of Molecular Biology 425 (2013) 2722–2736.","ama":"Rennella E, Cutuil T, Schanda P, et al. Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure. <i>Journal of Molecular Biology</i>. 2013;425(15):2722-2736. doi:<a href=\"https://doi.org/10.1016/j.jmb.2013.04.028\">10.1016/j.jmb.2013.04.028</a>","ista":"Rennella E, Cutuil T, Schanda P, Ayala I, Gabel F, Forge V, Corazza A, Esposito G, Brutscher B. 2013. Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure. Journal of Molecular Biology. 425(15), 2722–2736.","ieee":"E. Rennella <i>et al.</i>, “Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure,” <i>Journal of Molecular Biology</i>, vol. 425, no. 15. Elsevier, pp. 2722–2736, 2013.","apa":"Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Gabel, F., Forge, V., … Brutscher, B. (2013). Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2013.04.028\">https://doi.org/10.1016/j.jmb.2013.04.028</a>","chicago":"Rennella, E., T. Cutuil, Paul Schanda, I. Ayala, F. Gabel, V. Forge, A. Corazza, G. Esposito, and B. Brutscher. “Oligomeric States along the Folding Pathways of Β2-Microglobulin: Kinetics, Thermodynamics, and Structure.” <i>Journal of Molecular Biology</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.jmb.2013.04.028\">https://doi.org/10.1016/j.jmb.2013.04.028</a>."},"publisher":"Elsevier","publication_identifier":{"issn":["0022-2836"]},"language":[{"iso":"eng"}],"keyword":["Molecular Biology"],"article_processing_charge":"No","user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","status":"public","month":"08","date_updated":"2022-08-25T14:56:24Z","doi":"10.1016/j.jmb.2013.04.028","oa_version":"None","publication":"Journal of Molecular Biology","day":"09"},{"title":"The role of Nup98 in transcription regulation in healthy and diseased cells","extern":"1","pmid":1,"year":"2013","keyword":["Cell Biology"],"publication_identifier":{"issn":["0962-8924"]},"language":[{"iso":"eng"}],"article_type":"letter_note","publication":"Trends in Cell Biology","day":"01","doi":"10.1016/j.tcb.2012.10.013","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","date_created":"2022-04-07T07:50:33Z","external_id":{"pmid":["23246429"]},"publication_status":"published","abstract":[{"lang":"eng","text":"Nuclear pore complex (NPC) proteins are known for their critical roles in regulating nucleocytoplasmic traffic of macromolecules across the nuclear envelope. However, recent findings suggest that some nucleoporins (Nups), including Nup98, have additional functions in developmental gene regulation. Nup98, which exhibits transcription-dependent mobility at the NPC but can also bind chromatin away from the nuclear envelope, is frequently involved in chromosomal translocations in a subset of patients suffering from acute myeloid leukemia (AML). A common paradigm suggests that Nup98 translocations cause aberrant transcription when they are recuited to aberrant genomic loci. Importantly, this model fails to account for the potential loss of wild type (WT) Nup98 function in the presence of Nup98 translocation mutants. Here we examine how the cell might regulate Nup98 nucleoplasmic protein levels to control transcription in healthy cells. In addition, we discuss the possibility that dominant negative Nup98 fusion proteins disrupt the transcriptional activity of WT Nup98 in the nucleoplasm to drive AML."}],"scopus_import":"1","intvolume":"        23","date_published":"2013-03-01T00:00:00Z","author":[{"last_name":"Franks","full_name":"Franks, Tobias M.","first_name":"Tobias M."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"}],"volume":23,"page":"112-117","quality_controlled":"1","issue":"3","_id":"11083","article_processing_charge":"No","citation":{"chicago":"Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription Regulation in Healthy and Diseased Cells.” <i>Trends in Cell Biology</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">https://doi.org/10.1016/j.tcb.2012.10.013</a>.","ieee":"T. M. Franks and M. Hetzer, “The role of Nup98 in transcription regulation in healthy and diseased cells,” <i>Trends in Cell Biology</i>, vol. 23, no. 3. Elsevier, pp. 112–117, 2013.","apa":"Franks, T. M., &#38; Hetzer, M. (2013). The role of Nup98 in transcription regulation in healthy and diseased cells. <i>Trends in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">https://doi.org/10.1016/j.tcb.2012.10.013</a>","ista":"Franks TM, Hetzer M. 2013. The role of Nup98 in transcription regulation in healthy and diseased cells. Trends in Cell Biology. 23(3), 112–117.","ama":"Franks TM, Hetzer M. The role of Nup98 in transcription regulation in healthy and diseased cells. <i>Trends in Cell Biology</i>. 2013;23(3):112-117. doi:<a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">10.1016/j.tcb.2012.10.013</a>","mla":"Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription Regulation in Healthy and Diseased Cells.” <i>Trends in Cell Biology</i>, vol. 23, no. 3, Elsevier, 2013, pp. 112–17, doi:<a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">10.1016/j.tcb.2012.10.013</a>.","short":"T.M. Franks, M. Hetzer, Trends in Cell Biology 23 (2013) 112–117."},"publisher":"Elsevier","type":"journal_article","date_updated":"2022-07-18T08:45:34Z","oa_version":"None","status":"public","month":"03"},{"pmid":1,"extern":"1","year":"2013","title":"Protein homeostasis: Live long, won't prosper","day":"01","publication":"Nature Reviews Molecular Cell Biology","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","doi":"10.1038/nrm3496","language":[{"iso":"eng"}],"publication_identifier":{"issn":["1471-0072","1471-0080"]},"keyword":["Cell Biology","Molecular Biology"],"article_type":"original","page":"55-61","author":[{"last_name":"Toyama","first_name":"Brandon H.","full_name":"Toyama, Brandon H."},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W"}],"volume":14,"date_published":"2013-01-01T00:00:00Z","intvolume":"        14","_id":"11084","quality_controlled":"1","abstract":[{"lang":"eng","text":"Protein turnover is an effective way of maintaining a functional proteome, as old and potentially damaged polypeptides are destroyed and replaced by newly synthesized copies. An increasing number of intracellular proteins, however, have been identified that evade this turnover process and instead are maintained over a cell's lifetime. This diverse group of long-lived proteins might be particularly prone to accumulation of damage and thus have a crucial role in the functional deterioration of key regulatory processes during ageing."}],"publication_status":"published","date_created":"2022-04-07T07:50:43Z","external_id":{"pmid":["23258296"]},"scopus_import":"1","month":"01","status":"public","oa_version":"None","date_updated":"2022-07-18T08:37:53Z","publisher":"Springer Nature","citation":{"ista":"Toyama BH, Hetzer M. 2013. Protein homeostasis: Live long, won’t prosper. Nature Reviews Molecular Cell Biology. 14, 55–61.","ama":"Toyama BH, Hetzer M. Protein homeostasis: Live long, won’t prosper. <i>Nature Reviews Molecular Cell Biology</i>. 2013;14:55-61. doi:<a href=\"https://doi.org/10.1038/nrm3496\">10.1038/nrm3496</a>","mla":"Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t Prosper.” <i>Nature Reviews Molecular Cell Biology</i>, vol. 14, Springer Nature, 2013, pp. 55–61, doi:<a href=\"https://doi.org/10.1038/nrm3496\">10.1038/nrm3496</a>.","short":"B.H. Toyama, M. Hetzer, Nature Reviews Molecular Cell Biology 14 (2013) 55–61.","chicago":"Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t Prosper.” <i>Nature Reviews Molecular Cell Biology</i>. Springer Nature, 2013. <a href=\"https://doi.org/10.1038/nrm3496\">https://doi.org/10.1038/nrm3496</a>.","apa":"Toyama, B. H., &#38; Hetzer, M. (2013). Protein homeostasis: Live long, won’t prosper. <i>Nature Reviews Molecular Cell Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/nrm3496\">https://doi.org/10.1038/nrm3496</a>","ieee":"B. H. Toyama and M. Hetzer, “Protein homeostasis: Live long, won’t prosper,” <i>Nature Reviews Molecular Cell Biology</i>, vol. 14. Springer Nature, pp. 55–61, 2013."},"article_processing_charge":"No","type":"journal_article"},{"title":"Catastrophic nuclear envelope collapse in cancer cell micronuclei","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2013.06.007"}],"extern":"1","pmid":1,"year":"2013","keyword":["General Biochemistry","Genetics and Molecular Biology"],"oa":1,"language":[{"iso":"eng"}],"publication_identifier":{"issn":["0092-8674"]},"article_type":"original","day":"03","publication":"Cell","doi":"10.1016/j.cell.2013.06.007","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication_status":"published","date_created":"2022-04-07T07:50:51Z","external_id":{"pmid":["23827674"]},"abstract":[{"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.","lang":"eng"}],"scopus_import":"1","volume":154,"page":"47-60","author":[{"first_name":"Emily M.","full_name":"Hatch, Emily M.","last_name":"Hatch"},{"first_name":"Andrew H.","full_name":"Fischer, Andrew H.","last_name":"Fischer"},{"last_name":"Deerinck","full_name":"Deerinck, Thomas J.","first_name":"Thomas J."},{"full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","first_name":"Martin W","last_name":"HETZER"}],"intvolume":"       154","date_published":"2013-07-03T00:00:00Z","issue":"1","quality_controlled":"1","_id":"11085","article_processing_charge":"No","publisher":"Elsevier","citation":{"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>.","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.","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>","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>."},"type":"journal_article","oa_version":"Published Version","date_updated":"2022-07-18T08:45:47Z","month":"07","status":"public"},{"oa_version":"Published Version","date_updated":"2022-07-18T08:45:58Z","month":"02","status":"public","article_processing_charge":"No","publisher":"Public Library of Science","citation":{"ama":"Liang Y, Franks TM, Marchetto MC, Gage FH, Hetzer M. Dynamic association of NUP98 with the human genome. <i>PLoS Genetics</i>. 2013;9(2). doi:<a href=\"https://doi.org/10.1371/journal.pgen.1003308\">10.1371/journal.pgen.1003308</a>","ista":"Liang Y, Franks TM, Marchetto MC, Gage FH, Hetzer M. 2013. Dynamic association of NUP98 with the human genome. PLoS Genetics. 9(2), e1003308.","mla":"Liang, Yun, et al. “Dynamic Association of NUP98 with the Human Genome.” <i>PLoS Genetics</i>, vol. 9, no. 2, e1003308, Public Library of Science, 2013, doi:<a href=\"https://doi.org/10.1371/journal.pgen.1003308\">10.1371/journal.pgen.1003308</a>.","short":"Y. Liang, T.M. Franks, M.C. Marchetto, F.H. Gage, M. Hetzer, PLoS Genetics 9 (2013).","chicago":"Liang, Yun, Tobias M. Franks, Maria C. Marchetto, Fred H. Gage, and Martin Hetzer. “Dynamic Association of NUP98 with the Human Genome.” <i>PLoS Genetics</i>. Public Library of Science, 2013. <a href=\"https://doi.org/10.1371/journal.pgen.1003308\">https://doi.org/10.1371/journal.pgen.1003308</a>.","ieee":"Y. Liang, T. M. Franks, M. C. Marchetto, F. H. Gage, and M. Hetzer, “Dynamic association of NUP98 with the human genome,” <i>PLoS Genetics</i>, vol. 9, no. 2. Public Library of Science, 2013.","apa":"Liang, Y., Franks, T. M., Marchetto, M. C., Gage, F. H., &#38; Hetzer, M. (2013). Dynamic association of NUP98 with the human genome. <i>PLoS Genetics</i>. Public Library of Science. <a href=\"https://doi.org/10.1371/journal.pgen.1003308\">https://doi.org/10.1371/journal.pgen.1003308</a>"},"type":"journal_article","volume":9,"author":[{"first_name":"Yun","full_name":"Liang, Yun","last_name":"Liang"},{"full_name":"Franks, Tobias M.","first_name":"Tobias M.","last_name":"Franks"},{"last_name":"Marchetto","full_name":"Marchetto, Maria C.","first_name":"Maria C."},{"last_name":"Gage","full_name":"Gage, Fred H.","first_name":"Fred H."},{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"intvolume":"         9","date_published":"2013-02-28T00:00:00Z","issue":"2","quality_controlled":"1","_id":"11086","date_created":"2022-04-07T07:50:59Z","publication_status":"published","external_id":{"pmid":["23468646"]},"abstract":[{"lang":"eng","text":"Faithful execution of developmental gene expression programs occurs at multiple levels and involves many different components such as transcription factors, histone-modification enzymes, and mRNA processing proteins. Recent evidence suggests that nucleoporins, well known components that control nucleo-cytoplasmic trafficking, have wide-ranging functions in developmental gene regulation that potentially extend beyond their role in nuclear transport. Whether the unexpected role of nuclear pore proteins in transcription regulation, which initially has been described in fungi and flies, also applies to human cells is unknown. Here we show at a genome-wide level that the nuclear pore protein NUP98 associates with developmentally regulated genes active during human embryonic stem cell differentiation. Overexpression of a dominant negative fragment of NUP98 levels decreases expression levels of NUP98-bound genes. In addition, we identify two modes of developmental gene regulation by NUP98 that are differentiated by the spatial localization of NUP98 target genes. Genes in the initial stage of developmental induction can associate with NUP98 that is embedded in the nuclear pores at the nuclear periphery. Alternatively, genes that are highly induced can interact with NUP98 in the nuclear interior, away from the nuclear pores. This work demonstrates for the first time that NUP98 dynamically associates with the human genome during differentiation, revealing a role of a nuclear pore protein in regulating developmental gene expression programs."}],"scopus_import":"1","day":"28","publication":"PLoS Genetics","doi":"10.1371/journal.pgen.1003308","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","keyword":["Cancer Research","Genetics (clinical)","Genetics","Molecular Biology","Ecology","Evolution","Behavior and Systematics"],"oa":1,"publication_identifier":{"issn":["1553-7404"]},"language":[{"iso":"eng"}],"article_number":"e1003308","article_type":"original","extern":"1","pmid":1,"year":"2013","title":"Dynamic association of NUP98 with the human genome","main_file_link":[{"url":"https://doi.org/10.1371/journal.pgen.1003308","open_access":"1"}]},{"article_processing_charge":"No","publisher":"Elsevier","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.","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>","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>","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.","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.","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>."},"type":"journal_article","oa_version":"Published Version","date_updated":"2022-07-18T08:50:47Z","month":"08","status":"public","publication_status":"published","external_id":{"pmid":["23993091"]},"date_created":"2022-04-07T07:51:08Z","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"}],"scopus_import":"1","volume":154,"author":[{"last_name":"Toyama","first_name":"Brandon H.","full_name":"Toyama, Brandon H."},{"last_name":"Savas","full_name":"Savas, Jeffrey N.","first_name":"Jeffrey N."},{"last_name":"Park","first_name":"Sung Kyu","full_name":"Park, Sung Kyu"},{"first_name":"Michael S.","full_name":"Harris, Michael S.","last_name":"Harris"},{"last_name":"Ingolia","full_name":"Ingolia, Nicholas T.","first_name":"Nicholas T."},{"full_name":"Yates, John R.","first_name":"John R.","last_name":"Yates"},{"first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"page":"971-982","intvolume":"       154","date_published":"2013-08-29T00:00:00Z","issue":"5","quality_controlled":"1","_id":"11087","keyword":["General Biochemistry","Genetics and Molecular Biology"],"oa":1,"publication_identifier":{"issn":["0092-8674"]},"language":[{"iso":"eng"}],"article_type":"original","day":"29","publication":"Cell","doi":"10.1016/j.cell.2013.07.037","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","title":"Identification of long-lived proteins reveals exceptional stability of essential cellular structures","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2013.07.037"}],"extern":"1","pmid":1,"year":"2013"},{"scopus_import":"1","abstract":[{"lang":"eng","text":"The Nuclear Envelope (NE) contains over 100 different proteins that associate with nuclear components such as chromatin, the lamina and the transcription machinery. Mutations in genes encoding NE proteins have been shown to result in tissue-specific defects and disease, suggesting cell-type specific differences in NE composition and function. Consistent with these observations, recent studies have revealed unexpected functions for numerous NE associated proteins during cell differentiation and development. Here we review the latest insights into the roles played by the NE in cell differentiation, development, disease and aging, focusing primarily on inner nuclear membrane (INM) proteins and nuclear pore components."}],"publication_status":"published","external_id":{"pmid":["22995343"]},"date_created":"2022-04-07T07:51:37Z","_id":"11089","issue":"6","quality_controlled":"1","date_published":"2012-12-01T00:00:00Z","intvolume":"        24","volume":24,"author":[{"full_name":"Gomez-Cavazos, J Sebastian","first_name":"J Sebastian","last_name":"Gomez-Cavazos"},{"last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"page":"775-783","type":"journal_article","citation":{"mla":"Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “Outfits for Different Occasions: Tissue-Specific Roles of Nuclear Envelope Proteins.” <i>Current Opinion in Cell Biology</i>, vol. 24, no. 6, Elsevier, 2012, pp. 775–83, doi:<a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">10.1016/j.ceb.2012.08.008</a>.","short":"J.S. Gomez-Cavazos, M. Hetzer, Current Opinion in Cell Biology 24 (2012) 775–783.","ista":"Gomez-Cavazos JS, Hetzer M. 2012. Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. Current Opinion in Cell Biology. 24(6), 775–783.","ama":"Gomez-Cavazos JS, Hetzer M. Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. <i>Current Opinion in Cell Biology</i>. 2012;24(6):775-783. doi:<a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">10.1016/j.ceb.2012.08.008</a>","ieee":"J. S. Gomez-Cavazos and M. Hetzer, “Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins,” <i>Current Opinion in Cell Biology</i>, vol. 24, no. 6. Elsevier, pp. 775–783, 2012.","apa":"Gomez-Cavazos, J. S., &#38; Hetzer, M. (2012). Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">https://doi.org/10.1016/j.ceb.2012.08.008</a>","chicago":"Gomez-Cavazos, J Sebastian, and Martin Hetzer. “Outfits for Different Occasions: Tissue-Specific Roles of Nuclear Envelope Proteins.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2012. <a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">https://doi.org/10.1016/j.ceb.2012.08.008</a>."},"publisher":"Elsevier","article_processing_charge":"No","month":"12","status":"public","date_updated":"2022-07-18T08:38:47Z","oa_version":"None","title":"Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins","year":"2012","pmid":1,"extern":"1","article_type":"original","language":[{"iso":"eng"}],"publication_identifier":{"issn":["0955-0674"]},"keyword":["Cell Biology"],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","doi":"10.1016/j.ceb.2012.08.008","publication":"Current Opinion in Cell Biology","day":"01"},{"volume":149,"author":[{"last_name":"Hatch","full_name":"Hatch, Emily M.","first_name":"Emily M."},{"last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W"}],"page":"733-735","intvolume":"       149","date_published":"2012-05-11T00:00:00Z","issue":"4","quality_controlled":"1","_id":"11090","date_created":"2022-04-07T07:51:45Z","external_id":{"pmid":["22579277"]},"publication_status":"published","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."}],"scopus_import":"1","oa_version":"Published Version","date_updated":"2022-07-18T08:58:48Z","status":"public","month":"05","article_processing_charge":"No","publisher":"Elsevier","citation":{"ista":"Hatch EM, Hetzer M. 2012. RNP export by nuclear envelope budding. Cell. 149(4), 733–735.","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>","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.","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.","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>"},"type":"journal_article","extern":"1","pmid":1,"year":"2012","title":"RNP export by nuclear envelope budding","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2012.04.018","open_access":"1"}],"day":"11","publication":"Cell","doi":"10.1016/j.cell.2012.04.018","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa":1,"keyword":["General Biochemistry","Genetics and Molecular Biology"],"publication_identifier":{"issn":["0092-8674"]},"language":[{"iso":"eng"}],"article_type":"letter_note"},{"quality_controlled":"1","issue":"1","_id":"11091","date_published":"2012-01-01T00:00:00Z","intvolume":"         3","page":"88-100","volume":3,"author":[{"last_name":"Vargas","full_name":"Vargas, Jesse D.","first_name":"Jesse D."},{"first_name":"Emily M.","full_name":"Hatch, Emily M.","last_name":"Hatch"},{"first_name":"Daniel J.","full_name":"Anderson, Daniel J.","last_name":"Anderson"},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER"}],"scopus_import":"1","external_id":{"pmid":["22567193"]},"date_created":"2022-04-07T07:51:53Z","publication_status":"published","abstract":[{"text":"Neoplastic cells are often characterized by specific morphological abnormalities of the nuclear envelope (NE), which have been used for cancer diagnosis for more than a century. The NE is a double phospholipid bilayer that encapsulates the nuclear genome, regulates all nuclear trafficking of RNAs and proteins and prevents the passive diffusion of macromolecules between the nucleoplasm and the cytoplasm. Whether there is a consequence to the proper functioning of the cell and loss of structural integrity of the nucleus remains unclear. Using live cell imaging, we characterize a phenomenon wherein nuclei of several proliferating human cancer cell lines become temporarily ruptured during interphase. Strikingly, NE rupturing was associated with the mislocalization of nucleoplasmic and cytoplasmic proteins and, in the most extreme cases, the entrapment of cytoplasmic organelles in the nuclear interior. In addition, we observed the formation of micronuclei-like structures during interphase and the movement of chromatin out of the nuclear space. The frequency of these NE rupturing events was higher in cells in which the nuclear lamina, a network of intermediate filaments providing mechanical support to the NE, was not properly formed. Our data uncover the existence of a NE instability that has the potential to change the genomic landscape of cancer cells.","lang":"eng"}],"date_updated":"2022-07-18T08:52:53Z","oa_version":"None","status":"public","month":"01","type":"journal_article","article_processing_charge":"No","citation":{"ieee":"J. D. Vargas, E. M. Hatch, D. J. Anderson, and M. Hetzer, “Transient nuclear envelope rupturing during interphase in human cancer cells,” <i>Nucleus</i>, vol. 3, no. 1. Taylor &#38; Francis, pp. 88–100, 2012.","apa":"Vargas, J. D., Hatch, E. M., Anderson, D. J., &#38; Hetzer, M. (2012). Transient nuclear envelope rupturing during interphase in human cancer cells. <i>Nucleus</i>. Taylor &#38; Francis. <a href=\"https://doi.org/10.4161/nucl.18954\">https://doi.org/10.4161/nucl.18954</a>","chicago":"Vargas, Jesse D., Emily M. Hatch, Daniel J. Anderson, and Martin Hetzer. “Transient Nuclear Envelope Rupturing during Interphase in Human Cancer Cells.” <i>Nucleus</i>. Taylor &#38; Francis, 2012. <a href=\"https://doi.org/10.4161/nucl.18954\">https://doi.org/10.4161/nucl.18954</a>.","short":"J.D. Vargas, E.M. Hatch, D.J. Anderson, M. Hetzer, Nucleus 3 (2012) 88–100.","mla":"Vargas, Jesse D., et al. “Transient Nuclear Envelope Rupturing during Interphase in Human Cancer Cells.” <i>Nucleus</i>, vol. 3, no. 1, Taylor &#38; Francis, 2012, pp. 88–100, doi:<a href=\"https://doi.org/10.4161/nucl.18954\">10.4161/nucl.18954</a>.","ista":"Vargas JD, Hatch EM, Anderson DJ, Hetzer M. 2012. Transient nuclear envelope rupturing during interphase in human cancer cells. Nucleus. 3(1), 88–100.","ama":"Vargas JD, Hatch EM, Anderson DJ, Hetzer M. Transient nuclear envelope rupturing during interphase in human cancer cells. <i>Nucleus</i>. 2012;3(1):88-100. doi:<a href=\"https://doi.org/10.4161/nucl.18954\">10.4161/nucl.18954</a>"},"publisher":"Taylor & Francis","year":"2012","extern":"1","pmid":1,"title":"Transient nuclear envelope rupturing during interphase in human cancer cells","doi":"10.4161/nucl.18954","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication":"Nucleus","day":"01","article_type":"original","keyword":["Cell Biology"],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["1949-1034"],"eissn":["1949-1042"]}},{"page":"446-458","volume":22,"author":[{"first_name":"Maximiliano A.","full_name":"D'Angelo, Maximiliano A.","last_name":"D'Angelo"},{"last_name":"Gomez-Cavazos","full_name":"Gomez-Cavazos, J. Sebastian","first_name":"J. Sebastian"},{"last_name":"Mei","first_name":"Arianna","full_name":"Mei, Arianna"},{"last_name":"Lackner","full_name":"Lackner, Daniel H.","first_name":"Daniel H."},{"full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"date_published":"2012-01-19T00:00:00Z","intvolume":"        22","quality_controlled":"1","issue":"2","_id":"11093","date_created":"2022-04-07T07:52:10Z","external_id":{"pmid":["22264802"]},"publication_status":"published","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"}],"scopus_import":"1","oa_version":"Published Version","date_updated":"2022-07-18T08:53:16Z","status":"public","month":"01","article_processing_charge":"No","publisher":"Elsevier","citation":{"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>.","short":"M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental Cell 22 (2012) 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>","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.","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>","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.","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>."},"type":"journal_article","extern":"1","pmid":1,"year":"2012","title":"A change in nuclear pore complex composition regulates cell differentiation","main_file_link":[{"url":"https://doi.org/10.1016/j.devcel.2011.11.021","open_access":"1"}],"day":"19","publication":"Developmental Cell","doi":"10.1016/j.devcel.2011.11.021","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"oa":1,"publication_identifier":{"issn":["1534-5807"]},"language":[{"iso":"eng"}],"article_type":"original"},{"scopus_import":"1","publication_status":"published","date_created":"2022-04-07T07:52:18Z","external_id":{"pmid":["21727197"]},"abstract":[{"lang":"eng","text":"Nuclear pore complexes (NPCs) assemble at the end of mitosis during nuclear envelope (NE) reformation and into an intact NE as cells progress through interphase. Although recent studies have shown that NPC formation occurs by two different molecular mechanisms at two distinct cell cycle stages, little is known about the molecular players that mediate the fusion of the outer and inner nuclear membranes to form pores. In this paper, we provide evidence that the transmembrane nucleoporin (Nup), POM121, but not the Nup107–160 complex, is present at new pore assembly sites at a time that coincides with inner nuclear membrane (INM) and outer nuclear membrane (ONM) fusion. Overexpression of POM121 resulted in juxtaposition of the INM and ONM. Additionally, Sun1, an INM protein that is known to interact with the cytoskeleton, was specifically required for interphase assembly and localized with POM121 at forming pores. We propose a model in which POM121 and Sun1 interact transiently to promote early steps of interphase NPC assembly."}],"quality_controlled":"1","issue":"1","_id":"11094","intvolume":"       194","date_published":"2011-07-04T00:00:00Z","page":"27-37","volume":194,"author":[{"last_name":"Talamas","first_name":"Jessica A.","full_name":"Talamas, Jessica A."},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER"}],"type":"journal_article","article_processing_charge":"No","citation":{"ama":"Talamas JA, Hetzer M. POM121 and Sun1 play a role in early steps of interphase NPC assembly. <i>Journal of Cell Biology</i>. 2011;194(1):27-37. doi:<a href=\"https://doi.org/10.1083/jcb.201012154\">10.1083/jcb.201012154</a>","ista":"Talamas JA, Hetzer M. 2011. POM121 and Sun1 play a role in early steps of interphase NPC assembly. Journal of Cell Biology. 194(1), 27–37.","short":"J.A. Talamas, M. Hetzer, Journal of Cell Biology 194 (2011) 27–37.","mla":"Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in Early Steps of Interphase NPC Assembly.” <i>Journal of Cell Biology</i>, vol. 194, no. 1, Rockefeller University Press, 2011, pp. 27–37, doi:<a href=\"https://doi.org/10.1083/jcb.201012154\">10.1083/jcb.201012154</a>.","chicago":"Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in Early Steps of Interphase NPC Assembly.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2011. <a href=\"https://doi.org/10.1083/jcb.201012154\">https://doi.org/10.1083/jcb.201012154</a>.","ieee":"J. A. Talamas and M. Hetzer, “POM121 and Sun1 play a role in early steps of interphase NPC assembly,” <i>Journal of Cell Biology</i>, vol. 194, no. 1. Rockefeller University Press, pp. 27–37, 2011.","apa":"Talamas, J. A., &#38; Hetzer, M. (2011). POM121 and Sun1 play a role in early steps of interphase NPC assembly. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201012154\">https://doi.org/10.1083/jcb.201012154</a>"},"publisher":"Rockefeller University Press","date_updated":"2022-07-18T08:53:46Z","oa_version":"Published Version","status":"public","month":"07","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.201012154"}],"title":"POM121 and Sun1 play a role in early steps of interphase NPC assembly","year":"2011","extern":"1","pmid":1,"article_type":"original","keyword":["Cell Biology"],"oa":1,"language":[{"iso":"eng"}],"publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"doi":"10.1083/jcb.201012154","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication":"Journal of Cell Biology","day":"04"},{"day":"01","publication":"Current Opinion in Cell Biology","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","doi":"10.1016/j.ceb.2011.04.013","publication_identifier":{"issn":["0955-0674"]},"language":[{"iso":"eng"}],"keyword":["Cell Biology"],"article_type":"letter_note","pmid":1,"extern":"1","year":"2011","title":"Editorial overview","status":"public","month":"06","oa_version":"None","date_updated":"2022-07-18T08:39:40Z","publisher":"Elsevier","citation":{"ista":"Hetzer M, Cavalli G. 2011. Editorial overview. Current Opinion in Cell Biology. 23(3), 255–257.","ama":"Hetzer M, Cavalli G. Editorial overview. <i>Current Opinion in Cell Biology</i>. 2011;23(3):255-257. doi:<a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">10.1016/j.ceb.2011.04.013</a>","short":"M. Hetzer, G. Cavalli, Current Opinion in Cell Biology 23 (2011) 255–257.","mla":"Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 3, Elsevier, 2011, pp. 255–57, doi:<a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">10.1016/j.ceb.2011.04.013</a>.","chicago":"Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2011. <a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">https://doi.org/10.1016/j.ceb.2011.04.013</a>.","ieee":"M. Hetzer and G. Cavalli, “Editorial overview,” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 3. Elsevier, pp. 255–257, 2011.","apa":"Hetzer, M., &#38; Cavalli, G. (2011). Editorial overview. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">https://doi.org/10.1016/j.ceb.2011.04.013</a>"},"article_processing_charge":"No","type":"journal_article","volume":23,"page":"255-257","author":[{"orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER"},{"first_name":"Giacomo","full_name":"Cavalli, Giacomo","last_name":"Cavalli"}],"date_published":"2011-06-01T00:00:00Z","intvolume":"        23","_id":"11095","quality_controlled":"1","issue":"3","date_created":"2022-04-07T07:52:27Z","external_id":{"pmid":["21592757"]},"publication_status":"published","scopus_import":"1"},{"external_id":{"pmid":["21030234"]},"publication_status":"published","date_created":"2022-04-07T07:52:37Z","abstract":[{"text":"As the gatekeepers of the eukaryotic cell nucleus, nuclear pore complexes (NPCs) mediate all molecular trafficking between the nucleoplasm and the cytoplasm. In recent years, transport-independent functions of NPC components, nucleoporins, have been identified including roles in chromatin organization and gene regulation. Here, we summarize our current view of the NPC as a dynamic hub for the integration of chromatin regulation and nuclear trafficking and discuss the functional interplay between nucleoporins and the nuclear genome.","lang":"eng"}],"scopus_import":"1","date_published":"2011-02-01T00:00:00Z","intvolume":"        23","volume":23,"author":[{"first_name":"Yun","full_name":"Liang, Yun","last_name":"Liang"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"}],"page":"65-70","issue":"1","quality_controlled":"1","_id":"11096","article_processing_charge":"No","citation":{"chicago":"Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins and Chromatin.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2011. <a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">https://doi.org/10.1016/j.ceb.2010.09.008</a>.","ieee":"Y. Liang and M. Hetzer, “Functional interactions between nucleoporins and chromatin,” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 1. Elsevier, pp. 65–70, 2011.","apa":"Liang, Y., &#38; Hetzer, M. (2011). Functional interactions between nucleoporins and chromatin. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">https://doi.org/10.1016/j.ceb.2010.09.008</a>","ista":"Liang Y, Hetzer M. 2011. Functional interactions between nucleoporins and chromatin. Current Opinion in Cell Biology. 23(1), 65–70.","ama":"Liang Y, Hetzer M. Functional interactions between nucleoporins and chromatin. <i>Current Opinion in Cell Biology</i>. 2011;23(1):65-70. doi:<a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">10.1016/j.ceb.2010.09.008</a>","short":"Y. Liang, M. Hetzer, Current Opinion in Cell Biology 23 (2011) 65–70.","mla":"Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins and Chromatin.” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 1, Elsevier, 2011, pp. 65–70, doi:<a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">10.1016/j.ceb.2010.09.008</a>."},"publisher":"Elsevier","type":"journal_article","date_updated":"2022-07-18T08:53:48Z","oa_version":"None","month":"02","status":"public","title":"Functional interactions between nucleoporins and chromatin","extern":"1","pmid":1,"year":"2011","keyword":["Cell Biology"],"publication_identifier":{"issn":["0955-0674"]},"language":[{"iso":"eng"}],"article_type":"original","publication":"Current Opinion in Cell Biology","day":"01","doi":"10.1016/j.ceb.2010.09.008","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd"}]