[{"day":"01","publisher":"Cold Spring Harbor Laboratory","year":"2015","citation":{"ama":"Ibarra A, Hetzer M. Nuclear pore proteins and the control of genome functions. <i>Genes &#38; Development</i>. 2015;29(4):337-349. doi:<a href=\"https://doi.org/10.1101/gad.256495.114\">10.1101/gad.256495.114</a>","ista":"Ibarra A, Hetzer M. 2015. Nuclear pore proteins and the control of genome functions. Genes &#38; Development. 29(4), 337–349.","ieee":"A. Ibarra and M. Hetzer, “Nuclear pore proteins and the control of genome functions,” <i>Genes &#38; Development</i>, vol. 29, no. 4. Cold Spring Harbor Laboratory, pp. 337–349, 2015.","apa":"Ibarra, A., &#38; Hetzer, M. (2015). Nuclear pore proteins and the control of genome functions. <i>Genes &#38; Development</i>. Cold Spring Harbor Laboratory. <a href=\"https://doi.org/10.1101/gad.256495.114\">https://doi.org/10.1101/gad.256495.114</a>","chicago":"Ibarra, Arkaitz, and Martin Hetzer. “Nuclear Pore Proteins and the Control of Genome Functions.” <i>Genes &#38; Development</i>. Cold Spring Harbor Laboratory, 2015. <a href=\"https://doi.org/10.1101/gad.256495.114\">https://doi.org/10.1101/gad.256495.114</a>.","short":"A. Ibarra, M. Hetzer, Genes &#38; Development 29 (2015) 337–349.","mla":"Ibarra, Arkaitz, and Martin Hetzer. “Nuclear Pore Proteins and the Control of Genome Functions.” <i>Genes &#38; Development</i>, vol. 29, no. 4, Cold Spring Harbor Laboratory, 2015, pp. 337–49, doi:<a href=\"https://doi.org/10.1101/gad.256495.114\">10.1101/gad.256495.114</a>."},"status":"public","_id":"11076","oa_version":"Published Version","issue":"4","external_id":{"pmid":["25691464"]},"intvolume":"        29","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","abstract":[{"text":"Nuclear pore complexes (NPCs) are composed of several copies of ∼30 different proteins called nucleoporins (Nups). NPCs penetrate the nuclear envelope (NE) and regulate the nucleocytoplasmic trafficking of macromolecules. Beyond this vital role, NPC components influence genome functions in a transport-independent manner. Nups play an evolutionarily conserved role in gene expression regulation that, in metazoans, extends into the nuclear interior. Additionally, in proliferative cells, Nups play a crucial role in genome integrity maintenance and mitotic progression. Here we discuss genome-related functions of Nups and their impact on essential DNA metabolism processes such as transcription, chromosome duplication, and segregation.","lang":"eng"}],"date_updated":"2024-10-14T11:22:36Z","date_published":"2015-02-01T00:00:00Z","keyword":["Developmental Biology","Genetics"],"article_type":"original","fulldoi":"https://doi.org/10.1101/gad.256495.114","month":"02","page":"337-349","publication_status":"published","language":[{"iso":"eng"}],"volume":29,"quality_controlled":"1","article_processing_charge":"No","date_created":"2022-04-07T07:49:21Z","publication":"Genes & Development","author":[{"full_name":"Ibarra, Arkaitz","last_name":"Ibarra","first_name":"Arkaitz"},{"orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","full_name":"HETZER, Martin W"}],"scopus_import":"1","extern":"1","oa":1,"title":"Nuclear pore proteins and the control of genome functions","publication_identifier":{"issn":["0890-9369"],"eissn":["1549-5477"]},"pmid":1,"type":"journal_article","doi":"10.1101/gad.256495.114","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1101/gad.256495.114"}]},{"type":"journal_article","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1101/gad.260919.115"}],"doi":"10.1101/gad.260919.115","oa":1,"title":"The nucleoporin Nup153 regulates embryonic stem cell pluripotency through gene silencing","pmid":1,"publication_identifier":{"issn":["0890-9369"],"eissn":["1549-5477"]},"extern":"1","scopus_import":"1","author":[{"last_name":"Jacinto","full_name":"Jacinto, Filipe V.","first_name":"Filipe V."},{"first_name":"Chris","last_name":"Benner","full_name":"Benner, Chris"},{"full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","first_name":"Martin W"}],"publication":"Genes & Development","article_processing_charge":"No","date_created":"2022-04-07T07:49:31Z","quality_controlled":"1","publication_status":"published","language":[{"iso":"eng"}],"volume":29,"page":"1224-1238","month":"06","keyword":["Developmental Biology","Genetics"],"fulldoi":"https://doi.org/10.1101/gad.260919.115","article_type":"original","date_published":"2015-06-16T00:00:00Z","date_updated":"2024-10-14T11:22:47Z","abstract":[{"text":"Nucleoporins (Nups) are a family of proteins best known as the constituent building blocks of nuclear pore complexes (NPCs), membrane-embedded channels that mediate nuclear transport across the nuclear envelope. Recent evidence suggests that several Nups have additional roles in controlling the activation and silencing of developmental genes; however, the mechanistic details of these functions remain poorly understood. Here, we show that depletion of Nup153 in mouse embryonic stem cells (mESCs) causes the derepression of developmental genes and induction of early differentiation. This loss of stem cell identity is not associated with defects in the nuclear import of key pluripotency factors. Rather, Nup153 binds around the transcriptional start site (TSS) of developmental genes and mediates the recruitment of the polycomb-repressive complex 1 (PRC1) to a subset of its target loci. Our results demonstrate a chromatin-associated role of Nup153 in maintaining stem cell pluripotency by functioning in mammalian epigenetic gene silencing.","lang":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","intvolume":"        29","issue":"12","external_id":{"pmid":["26080816"]},"oa_version":"Published Version","_id":"11077","status":"public","publisher":"Cold Spring Harbor Laboratory","year":"2015","citation":{"ama":"Jacinto FV, Benner C, Hetzer M. The nucleoporin Nup153 regulates embryonic stem cell pluripotency through gene silencing. <i>Genes &#38; Development</i>. 2015;29(12):1224-1238. doi:<a href=\"https://doi.org/10.1101/gad.260919.115\">10.1101/gad.260919.115</a>","ista":"Jacinto FV, Benner C, Hetzer M. 2015. The nucleoporin Nup153 regulates embryonic stem cell pluripotency through gene silencing. Genes &#38; Development. 29(12), 1224–1238.","ieee":"F. V. Jacinto, C. Benner, and M. Hetzer, “The nucleoporin Nup153 regulates embryonic stem cell pluripotency through gene silencing,” <i>Genes &#38; Development</i>, vol. 29, no. 12. Cold Spring Harbor Laboratory, pp. 1224–1238, 2015.","apa":"Jacinto, F. V., Benner, C., &#38; Hetzer, M. (2015). The nucleoporin Nup153 regulates embryonic stem cell pluripotency through gene silencing. <i>Genes &#38; Development</i>. Cold Spring Harbor Laboratory. <a href=\"https://doi.org/10.1101/gad.260919.115\">https://doi.org/10.1101/gad.260919.115</a>","chicago":"Jacinto, Filipe V., Chris Benner, and Martin Hetzer. “The Nucleoporin Nup153 Regulates Embryonic Stem Cell Pluripotency through Gene Silencing.” <i>Genes &#38; Development</i>. Cold Spring Harbor Laboratory, 2015. <a href=\"https://doi.org/10.1101/gad.260919.115\">https://doi.org/10.1101/gad.260919.115</a>.","mla":"Jacinto, Filipe V., et al. “The Nucleoporin Nup153 Regulates Embryonic Stem Cell Pluripotency through Gene Silencing.” <i>Genes &#38; Development</i>, vol. 29, no. 12, Cold Spring Harbor Laboratory, 2015, pp. 1224–38, doi:<a href=\"https://doi.org/10.1101/gad.260919.115\">10.1101/gad.260919.115</a>.","short":"F.V. Jacinto, C. Benner, M. Hetzer, Genes &#38; Development 29 (2015) 1224–1238."},"day":"16"},{"page":"705-718","language":[{"iso":"eng"}],"volume":17,"publication_status":"published","month":"12","date_created":"2022-04-07T07:49:51Z","article_processing_charge":"No","quality_controlled":"1","scopus_import":"1","publication":"Cell Stem Cell","author":[{"first_name":"Jerome","last_name":"Mertens","full_name":"Mertens, Jerome"},{"last_name":"Paquola","full_name":"Paquola, Apuã C.M.","first_name":"Apuã C.M."},{"last_name":"Ku","full_name":"Ku, Manching","first_name":"Manching"},{"first_name":"Emily","full_name":"Hatch, Emily","last_name":"Hatch"},{"last_name":"Böhnke","full_name":"Böhnke, Lena","first_name":"Lena"},{"last_name":"Ladjevardi","full_name":"Ladjevardi, Shauheen","first_name":"Shauheen"},{"first_name":"Sean","last_name":"McGrath","full_name":"McGrath, Sean"},{"last_name":"Campbell","full_name":"Campbell, Benjamin","first_name":"Benjamin"},{"first_name":"Hyungjun","last_name":"Lee","full_name":"Lee, Hyungjun"},{"full_name":"Herdy, Joseph R.","last_name":"Herdy","first_name":"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","last_name":"Winkler","first_name":"Jürgen"},{"last_name":"Yao","full_name":"Yao, Jun","first_name":"Jun"},{"orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"},{"full_name":"Gage, Fred H.","last_name":"Gage","first_name":"Fred H."}],"publication_identifier":{"issn":["1934-5909"]},"pmid":1,"oa":1,"title":"Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.stem.2015.09.001"}],"doi":"10.1016/j.stem.2015.09.001","type":"journal_article","extern":"1","_id":"11079","status":"public","oa_version":"Published Version","day":"03","citation":{"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>","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.","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>."},"year":"2015","publisher":"Elsevier","external_id":{"pmid":["26456686"]},"issue":"6","intvolume":"        17","date_updated":"2022-07-18T08:44:21Z","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","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"}],"date_published":"2015-12-03T00:00:00Z","fulldoi":"https://doi.org/10.1016/j.stem.2015.09.001","article_type":"original","keyword":["Cell Biology","Genetics","Molecular Medicine"]},{"scopus_import":"1","author":[{"first_name":"P. M.","last_name":"Kraus","full_name":"Kraus, P. M."},{"first_name":"O. I.","full_name":"Tolstikhin, O. I.","last_name":"Tolstikhin"},{"full_name":"Baykusheva, Denitsa Rangelova","id":"71b4d059-2a03-11ee-914d-dfa3beed6530","last_name":"Baykusheva","first_name":"Denitsa Rangelova"},{"first_name":"A.","last_name":"Rupenyan","full_name":"Rupenyan, A."},{"first_name":"J.","last_name":"Schneider","full_name":"Schneider, J."},{"full_name":"Bisgaard, C. Z.","last_name":"Bisgaard","first_name":"C. Z."},{"full_name":"Morishita, T.","last_name":"Morishita","first_name":"T."},{"first_name":"F.","last_name":"Jensen","full_name":"Jensen, F."},{"full_name":"Madsen, L. B.","last_name":"Madsen","first_name":"L. B."},{"first_name":"H. J.","full_name":"Wörner, H. J.","last_name":"Wörner"}],"publication":"Nature Communications","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms8039"}],"doi":"10.1038/ncomms8039","type":"journal_article","publication_identifier":{"eissn":["2041-1723"]},"pmid":1,"title":"Observation of laser-induced electronic structure in oriented polyatomic molecules","oa":1,"extern":"1","article_number":"7039","volume":6,"language":[{"iso":"eng"}],"publication_status":"published","month":"05","date_created":"2023-08-10T06:38:01Z","article_processing_charge":"No","quality_controlled":"1","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"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.1038/ncomms8039","article_type":"original","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"date_published":"2015-05-05T00:00:00Z","oa_version":"Published Version","_id":"14016","status":"public","year":"2015","citation":{"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>.","mla":"Kraus, P. M., et al. “Observation of Laser-Induced Electronic Structure in Oriented Polyatomic Molecules.” <i>Nature Communications</i>, vol. 6, 7039, Springer Nature, 2015, doi:<a href=\"https://doi.org/10.1038/ncomms8039\">10.1038/ncomms8039</a>.","short":"P.M. Kraus, O.I. Tolstikhin, D.R. Baykusheva, A. Rupenyan, J. Schneider, C.Z. Bisgaard, T. Morishita, F. Jensen, L.B. Madsen, H.J. Wörner, Nature Communications 6 (2015).","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>","ista":"Kraus PM, Tolstikhin OI, Baykusheva DR, Rupenyan A, Schneider J, Bisgaard CZ, Morishita T, Jensen F, Madsen LB, Wörner HJ. 2015. Observation of laser-induced electronic structure in oriented polyatomic molecules. Nature Communications. 6, 7039.","apa":"Kraus, P. M., Tolstikhin, O. I., Baykusheva, D. R., Rupenyan, A., Schneider, J., Bisgaard, C. Z., … Wörner, H. J. (2015). Observation of laser-induced electronic structure in oriented polyatomic molecules. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms8039\">https://doi.org/10.1038/ncomms8039</a>","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."},"publisher":"Springer Nature","day":"05","intvolume":"         6","external_id":{"pmid":["25940229"]}},{"scopus_import":"1","author":[{"first_name":"Peixiang","last_name":"Ma","full_name":"Ma, Peixiang"},{"first_name":"Yi","last_name":"Xue","full_name":"Xue, Yi"},{"last_name":"Coquelle","full_name":"Coquelle, Nicolas","first_name":"Nicolas"},{"first_name":"Jens D.","full_name":"Haller, Jens D.","last_name":"Haller"},{"last_name":"Yuwen","full_name":"Yuwen, Tairan","first_name":"Tairan"},{"last_name":"Ayala","full_name":"Ayala, Isabel","first_name":"Isabel"},{"first_name":"Oleg","full_name":"Mikhailovskii, Oleg","last_name":"Mikhailovskii"},{"last_name":"Willbold","full_name":"Willbold, Dieter","first_name":"Dieter"},{"full_name":"Colletier, Jacques-Philippe","last_name":"Colletier","first_name":"Jacques-Philippe"},{"last_name":"Skrynnikov","full_name":"Skrynnikov, Nikolai R.","first_name":"Nikolai R."},{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606"}],"publication":"Nature Communications","doi":"10.1038/ncomms9361","main_file_link":[{"url":"https://doi.org/10.1038/ncomms9361","open_access":"1"}],"type":"journal_article","publication_identifier":{"issn":["2041-1723"]},"oa":1,"title":"Observing the overall rocking motion of a protein in a crystal","extern":"1","article_number":"8361","volume":6,"language":[{"iso":"eng"}],"publication_status":"published","month":"10","date_created":"2020-09-18T10:07:36Z","article_processing_charge":"Yes","quality_controlled":"1","date_updated":"2025-01-22T14:39:22Z","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."}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.1038/ncomms9361","article_type":"original","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"date_published":"2015-10-05T00:00:00Z","OA_type":"gold","OA_place":"publisher","oa_version":"Published Version","status":"public","_id":"8456","year":"2015","citation":{"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.","ama":"Ma P, Xue Y, Coquelle N, et al. Observing the overall rocking motion of a protein in a crystal. <i>Nature Communications</i>. 2015;6. doi:<a href=\"https://doi.org/10.1038/ncomms9361\">10.1038/ncomms9361</a>","ista":"Ma P, Xue Y, Coquelle N, Haller JD, Yuwen T, Ayala I, Mikhailovskii O, Willbold D, Colletier J-P, Skrynnikov NR, Schanda P. 2015. Observing the overall rocking motion of a protein in a crystal. Nature Communications. 6, 8361.","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).","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>."},"publisher":"Springer Nature","day":"05","intvolume":"         6"},{"intvolume":"       156","issue":"5","external_id":{"pmid":["24581486"]},"publisher":"Elsevier","year":"2014","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>.","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.","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>","ista":"Buchwalter A, Hetzer M. 2014. Nuclear pores set the speed limit for mitosis. Cell. 156(5), 868–869.","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>"},"day":"27","oa_version":"Published Version","_id":"11080","status":"public","keyword":["General Biochemistry","Genetics and Molecular Biology"],"fulldoi":"https://doi.org/10.1016/j.cell.2014.02.004","article_type":"original","date_published":"2014-02-27T00:00:00Z","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."}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2024-10-14T11:23:12Z","quality_controlled":"1","article_processing_charge":"No","date_created":"2022-04-07T07:50:04Z","month":"02","publication_status":"published","language":[{"iso":"eng"}],"volume":156,"page":"868-869","extern":"1","type":"journal_article","doi":"10.1016/j.cell.2014.02.004","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","oa":1,"pmid":1,"publication_identifier":{"issn":["0092-8674"]},"author":[{"first_name":"Abigail","last_name":"Buchwalter","full_name":"Buchwalter, Abigail"},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"}],"publication":"Cell","scopus_import":"1"},{"extern":"1","article_number":"3588","doi":"10.1038/ncomms4588","main_file_link":[{"url":"https://doi.org/10.1038/ncomms4588","open_access":"1"}],"type":"journal_article","pmid":1,"publication_identifier":{"eissn":["2041-1723"]},"oa":1,"title":"Nanoporous frameworks exhibiting multiple stimuli responsiveness","author":[{"first_name":"Pintu K.","full_name":"Kundu, Pintu K.","last_name":"Kundu"},{"first_name":"Gregory L.","full_name":"Olsen, Gregory L.","last_name":"Olsen"},{"last_name":"Kiss","full_name":"Kiss, Vladimir","first_name":"Vladimir"},{"id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn","full_name":"Klajn, Rafal","first_name":"Rafal"}],"publication":"Nature Communications","scopus_import":"1","quality_controlled":"1","date_created":"2023-08-01T09:46:27Z","article_processing_charge":"No","month":"04","language":[{"iso":"eng"}],"volume":5,"publication_status":"published","article_type":"original","fulldoi":"https://doi.org/10.1038/ncomms4588","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"date_published":"2014-04-07T00:00:00Z","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"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2024-10-14T12:20:30Z","intvolume":"         5","external_id":{"pmid":["24709950"]},"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>","ista":"Kundu PK, Olsen GL, Kiss V, Klajn R. 2014. Nanoporous frameworks exhibiting multiple stimuli responsiveness. Nature Communications. 5, 3588.","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>","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).","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>."},"year":"2014","publisher":"Springer Nature","day":"07","oa_version":"Published Version","status":"public","_id":"13402"},{"oa_version":"Published Version","status":"public","_id":"11085","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>.","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."},"year":"2013","day":"03","intvolume":"       154","issue":"1","external_id":{"pmid":["23827674"]},"date_updated":"2024-10-14T11:24:29Z","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"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","keyword":["General Biochemistry","Genetics and Molecular Biology"],"fulldoi":"https://doi.org/10.1016/j.cell.2013.06.007","article_type":"original","date_published":"2013-07-03T00:00:00Z","publication_status":"published","volume":154,"language":[{"iso":"eng"}],"page":"47-60","month":"07","article_processing_charge":"No","date_created":"2022-04-07T07:50:51Z","quality_controlled":"1","scopus_import":"1","author":[{"first_name":"Emily M.","last_name":"Hatch","full_name":"Hatch, Emily M."},{"first_name":"Andrew H.","full_name":"Fischer, Andrew H.","last_name":"Fischer"},{"last_name":"Deerinck","full_name":"Deerinck, Thomas J.","first_name":"Thomas J."},{"orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"publication":"Cell","type":"journal_article","doi":"10.1016/j.cell.2013.06.007","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2013.06.007","open_access":"1"}],"title":"Catastrophic nuclear envelope collapse in cancer cell micronuclei","oa":1,"pmid":1,"publication_identifier":{"issn":["0092-8674"]},"extern":"1"},{"intvolume":"         9","issue":"2","external_id":{"pmid":["23468646"]},"oa_version":"Published Version","_id":"11086","status":"public","publisher":"Public Library of Science","citation":{"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>.","short":"Y. Liang, T.M. Franks, M.C. Marchetto, F.H. Gage, M. Hetzer, PLoS Genetics 9 (2013).","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>.","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.","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>","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."},"year":"2013","day":"28","keyword":["Cancer Research","Genetics (clinical)","Genetics","Molecular Biology","Ecology","Evolution","Behavior and Systematics"],"fulldoi":"https://doi.org/10.1371/journal.pgen.1003308","article_type":"original","date_published":"2013-02-28T00:00:00Z","date_updated":"2024-10-14T11:24:40Z","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."}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","date_created":"2022-04-07T07:50:59Z","quality_controlled":"1","publication_status":"published","language":[{"iso":"eng"}],"volume":9,"month":"02","type":"journal_article","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1371/journal.pgen.1003308"}],"doi":"10.1371/journal.pgen.1003308","title":"Dynamic association of NUP98 with the human genome","oa":1,"pmid":1,"publication_identifier":{"issn":["1553-7404"]},"extern":"1","article_number":"e1003308","scopus_import":"1","author":[{"first_name":"Yun","last_name":"Liang","full_name":"Liang, Yun"},{"first_name":"Tobias M.","last_name":"Franks","full_name":"Franks, Tobias M."},{"full_name":"Marchetto, Maria C.","last_name":"Marchetto","first_name":"Maria C."},{"first_name":"Fred H.","last_name":"Gage","full_name":"Gage, Fred H."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","full_name":"HETZER, Martin W","first_name":"Martin W","orcid":"0000-0002-2111-992X"}],"publication":"PLoS Genetics"},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","abstract":[{"lang":"eng","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."}],"date_updated":"2026-07-28T10:15:26Z","OA_place":"publisher","date_published":"2013-08-29T00:00:00Z","OA_type":"free access","fulldoi":"https://doi.org/10.1016/j.cell.2013.07.037","article_type":"original","keyword":["General Biochemistry","Genetics and Molecular Biology"],"das_tickbox":"1","day":"29","citation":{"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>","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.","ama":"Toyama BH, Savas JN, Park SK, et al. Identification of long-lived proteins reveals exceptional stability of essential cellular structures. <i>Cell</i>. 2013;154(5):971-982. doi:<a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">10.1016/j.cell.2013.07.037</a>","mla":"Toyama, Brandon H., et al. “Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures.” <i>Cell</i>, vol. 154, no. 5, Elsevier, 2013, pp. 971–82, doi:<a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">10.1016/j.cell.2013.07.037</a>.","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.","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>."},"year":"2013","publisher":"Elsevier","_id":"11087","status":"public","oa_version":"Published Version","external_id":{"pmid":["23993091"]},"issue":"5","intvolume":"       154","publication":"Cell","author":[{"first_name":"Brandon H.","full_name":"Toyama, Brandon H.","last_name":"Toyama"},{"first_name":"Jeffrey N.","last_name":"Savas","full_name":"Savas, Jeffrey N."},{"last_name":"Park","full_name":"Park, Sung Kyu","first_name":"Sung Kyu"},{"last_name":"Harris","full_name":"Harris, Michael S.","first_name":"Michael S."},{"first_name":"Nicholas T.","last_name":"Ingolia","full_name":"Ingolia, Nicholas T."},{"full_name":"Yates, John R.","last_name":"Yates","first_name":"John R."},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W"}],"scopus_import":"1","extern":"1","pmid":1,"publication_identifier":{"issn":["0092-8674"]},"oa":1,"title":"Identification of long-lived proteins reveals exceptional stability of essential cellular structures","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2013.07.037","open_access":"1"}],"doi":"10.1016/j.cell.2013.07.037","type":"journal_article","month":"08","page":"971-982","volume":154,"language":[{"iso":"eng"}],"department":[{"_id":"MaHe"}],"publication_status":"published","quality_controlled":"1","date_created":"2022-04-07T07:51:08Z","article_processing_charge":"No"},{"month":"05","page":"733-735","publication_status":"published","volume":149,"language":[{"iso":"eng"}],"quality_controlled":"1","article_processing_charge":"No","date_created":"2022-04-07T07:51:45Z","publication":"Cell","author":[{"full_name":"Hatch, Emily M.","last_name":"Hatch","first_name":"Emily M."},{"full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","orcid":"0000-0002-2111-992X"}],"scopus_import":"1","extern":"1","oa":1,"title":"RNP export by nuclear envelope budding","publication_identifier":{"issn":["0092-8674"]},"pmid":1,"type":"journal_article","doi":"10.1016/j.cell.2012.04.018","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2012.04.018","open_access":"1"}],"day":"11","publisher":"Elsevier","citation":{"ama":"Hatch EM, Hetzer M. RNP export by nuclear envelope budding. <i>Cell</i>. 2012;149(4):733-735. doi:<a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">10.1016/j.cell.2012.04.018</a>","ista":"Hatch EM, Hetzer M. 2012. RNP export by nuclear envelope budding. Cell. 149(4), 733–735.","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>","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."},"year":"2012","status":"public","_id":"11090","oa_version":"Published Version","issue":"4","external_id":{"pmid":["22579277"]},"intvolume":"       149","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","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."}],"date_updated":"2024-10-14T11:25:24Z","date_published":"2012-05-11T00:00:00Z","keyword":["General Biochemistry","Genetics and Molecular Biology"],"fulldoi":"https://doi.org/10.1016/j.cell.2012.04.018","article_type":"letter_note"},{"intvolume":"        22","external_id":{"pmid":["22264802"]},"issue":"2","oa_version":"Published Version","_id":"11093","status":"public","citation":{"ista":"D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. 2012. A change in nuclear pore complex composition regulates cell differentiation. Developmental Cell. 22(2), 446–458.","ama":"D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. A change in nuclear pore complex composition regulates cell differentiation. <i>Developmental Cell</i>. 2012;22(2):446-458. doi:<a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">10.1016/j.devcel.2011.11.021</a>","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>.","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."},"year":"2012","publisher":"Elsevier","day":"19","fulldoi":"https://doi.org/10.1016/j.devcel.2011.11.021","article_type":"original","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"date_published":"2012-01-19T00:00:00Z","date_updated":"2024-10-14T11:26:00Z","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"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2022-04-07T07:52:10Z","article_processing_charge":"No","quality_controlled":"1","volume":22,"language":[{"iso":"eng"}],"publication_status":"published","page":"446-458","month":"01","main_file_link":[{"url":"https://doi.org/10.1016/j.devcel.2011.11.021","open_access":"1"}],"doi":"10.1016/j.devcel.2011.11.021","type":"journal_article","pmid":1,"publication_identifier":{"issn":["1534-5807"]},"oa":1,"title":"A change in nuclear pore complex composition regulates cell differentiation","extern":"1","scopus_import":"1","author":[{"first_name":"Maximiliano A.","full_name":"D'Angelo, Maximiliano A.","last_name":"D'Angelo"},{"first_name":"J. Sebastian","full_name":"Gomez-Cavazos, J. Sebastian","last_name":"Gomez-Cavazos"},{"first_name":"Arianna","last_name":"Mei","full_name":"Mei, Arianna"},{"first_name":"Daniel H.","last_name":"Lackner","full_name":"Lackner, Daniel H."},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"}],"publication":"Developmental Cell"},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","abstract":[{"text":"Eukaryotic cell function depends on the physical separation of nucleoplasmic and cytoplasmic components by the nuclear envelope (NE). Molecular communication between the two compartments involves active, signal-mediated trafficking, a function that is exclusively performed by nuclear pore complexes (NPCs). The individual NPC components and the mechanisms that are involved in nuclear trafficking are well documented and have become textbook knowledge. However, in addition to their roles as nuclear gatekeepers, NPC components-nucleoporins-have been shown to have critical roles in chromatin organization and gene regulation. These findings have sparked new enthusiasm to study the roles of this multiprotein complex in nuclear organization and explore novel functions that in some cases appear to go beyond a role in transport. Here, we discuss our present view of NPC biogenesis, which is tightly linked to proper cell cycle progression and cell differentiation. In addition, we summarize new data suggesting that NPCs represent dynamic hubs for the integration of gene regulation and nuclear transport processes.","lang":"eng"}],"date_updated":"2024-10-14T11:27:48Z","date_published":"2011-04-18T00:00:00Z","keyword":["Genetics","Molecular Biology","Biochemistry"],"fulldoi":"https://doi.org/10.1101/sqb.2010.75.059","article_type":"original","day":"18","publisher":"Cold Spring Harbor Laboratory Press","year":"2011","citation":{"ama":"Capelson M, Doucet C, Hetzer M. Nuclear pore complexes: Guardians of the nuclear genome. <i>Cold Spring Harbor Symposia on Quantitative Biology</i>. 2011;75:585-597. doi:<a href=\"https://doi.org/10.1101/sqb.2010.75.059\">10.1101/sqb.2010.75.059</a>","ista":"Capelson M, Doucet C, Hetzer M. 2011. Nuclear pore complexes: Guardians of the nuclear genome. Cold Spring Harbor Symposia on Quantitative Biology. 75, 585–597.","apa":"Capelson, M., Doucet, C., &#38; Hetzer, M. (2011). Nuclear pore complexes: Guardians of the nuclear genome. <i>Cold Spring Harbor Symposia on Quantitative Biology</i>. Cold Spring Harbor Laboratory Press. <a href=\"https://doi.org/10.1101/sqb.2010.75.059\">https://doi.org/10.1101/sqb.2010.75.059</a>","ieee":"M. Capelson, C. Doucet, and M. Hetzer, “Nuclear pore complexes: Guardians of the nuclear genome,” <i>Cold Spring Harbor Symposia on Quantitative Biology</i>, vol. 75. Cold Spring Harbor Laboratory Press, pp. 585–597, 2011.","chicago":"Capelson, M., C. Doucet, and Martin Hetzer. “Nuclear Pore Complexes: Guardians of the Nuclear Genome.” <i>Cold Spring Harbor Symposia on Quantitative Biology</i>. Cold Spring Harbor Laboratory Press, 2011. <a href=\"https://doi.org/10.1101/sqb.2010.75.059\">https://doi.org/10.1101/sqb.2010.75.059</a>.","mla":"Capelson, M., et al. “Nuclear Pore Complexes: Guardians of the Nuclear Genome.” <i>Cold Spring Harbor Symposia on Quantitative Biology</i>, vol. 75, Cold Spring Harbor Laboratory Press, 2011, pp. 585–97, doi:<a href=\"https://doi.org/10.1101/sqb.2010.75.059\">10.1101/sqb.2010.75.059</a>.","short":"M. Capelson, C. Doucet, M. Hetzer, Cold Spring Harbor Symposia on Quantitative Biology 75 (2011) 585–597."},"status":"public","_id":"11100","oa_version":"None","external_id":{"pmid":["21502404"]},"intvolume":"        75","publication":"Cold Spring Harbor Symposia on Quantitative Biology","author":[{"first_name":"M.","last_name":"Capelson","full_name":"Capelson, M."},{"full_name":"Doucet, C.","last_name":"Doucet","first_name":"C."},{"orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"}],"scopus_import":"1","extern":"1","title":"Nuclear pore complexes: Guardians of the nuclear genome","publication_identifier":{"isbn":["9781936113071"],"issn":["0091-7451","1943-4456"]},"pmid":1,"type":"journal_article","doi":"10.1101/sqb.2010.75.059","month":"04","page":"585-597","publication_status":"published","volume":75,"language":[{"iso":"eng"}],"quality_controlled":"1","article_processing_charge":"No","date_created":"2022-04-07T07:53:18Z"},{"publication":"Cold Spring Harbor Perspectives in Biology","author":[{"orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","full_name":"HETZER, Martin W"}],"scopus_import":"1","extern":"1","pmid":1,"publication_identifier":{"issn":["1943-0264"]},"title":"The nuclear envelope","doi":"10.1101/cshperspect.a000539","type":"journal_article","month":"02","page":"a000539-a000539","volume":2,"language":[{"iso":"eng"}],"publication_status":"published","quality_controlled":"1","date_created":"2022-04-07T07:52:49Z","article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","abstract":[{"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.","lang":"eng"}],"date_updated":"2024-10-14T11:26:41Z","date_published":"2010-02-03T00:00:00Z","fulldoi":"https://doi.org/10.1101/cshperspect.a000539","article_type":"original","keyword":["General Biochemistry","Genetics and Molecular Biology"],"day":"03","year":"2010","citation":{"ista":"Hetzer M. 2010. The nuclear envelope. Cold Spring Harbor Perspectives in Biology. 2(3), a000539–a000539.","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>","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.","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>","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>.","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>."},"publisher":"Cold Spring Harbor Laboratory","status":"public","_id":"11097","oa_version":"None","external_id":{"pmid":["20300205"]},"issue":"3","intvolume":"         2"},{"external_id":{"pmid":["20721671"]},"intvolume":"       119","day":"01","publisher":"Springer Nature","citation":{"ieee":"C. M. Doucet and M. Hetzer, “Nuclear pore biogenesis into an intact nuclear envelope,” <i>Chromosoma</i>, vol. 119. Springer Nature, pp. 469–477, 2010.","apa":"Doucet, C. M., &#38; Hetzer, M. (2010). Nuclear pore biogenesis into an intact nuclear envelope. <i>Chromosoma</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s00412-010-0289-2\">https://doi.org/10.1007/s00412-010-0289-2</a>","ista":"Doucet CM, Hetzer M. 2010. Nuclear pore biogenesis into an intact nuclear envelope. Chromosoma. 119, 469–477.","ama":"Doucet CM, Hetzer M. Nuclear pore biogenesis into an intact nuclear envelope. <i>Chromosoma</i>. 2010;119:469-477. doi:<a href=\"https://doi.org/10.1007/s00412-010-0289-2\">10.1007/s00412-010-0289-2</a>","short":"C.M. Doucet, M. Hetzer, Chromosoma 119 (2010) 469–477.","mla":"Doucet, Christine M., and Martin Hetzer. “Nuclear Pore Biogenesis into an Intact Nuclear Envelope.” <i>Chromosoma</i>, vol. 119, Springer Nature, 2010, pp. 469–77, doi:<a href=\"https://doi.org/10.1007/s00412-010-0289-2\">10.1007/s00412-010-0289-2</a>.","chicago":"Doucet, Christine M., and Martin Hetzer. “Nuclear Pore Biogenesis into an Intact Nuclear Envelope.” <i>Chromosoma</i>. Springer Nature, 2010. <a href=\"https://doi.org/10.1007/s00412-010-0289-2\">https://doi.org/10.1007/s00412-010-0289-2</a>."},"year":"2010","_id":"11099","status":"public","oa_version":"None","date_published":"2010-10-01T00:00:00Z","keyword":["Genetics (clinical)","Genetics"],"fulldoi":"https://doi.org/10.1007/s00412-010-0289-2","article_type":"review","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","abstract":[{"text":"Nuclear pore complexes (NPCs) serve as transport channels across the nuclear membrane, a double lipid bilayer that physically separates the nucleoplasm and cytoplasm of eukaryotic cells. New evidence suggests that the multiprotein nuclear pores also play a role in chromatin organization and gene expression. Given the importance of NPC function, it is not surprising that a growing list of human diseases and developmental defects have been linked to its malfunction. In order to fully understand the functional repertoire of NPCs and their essential role for nuclear organization, it is critical to determine the sequence of events that lead to the formation of nuclear pores. This is particularly relevant since NPC number, and possibly composition, are tightly linked to metabolic activity. Most of our knowledge is derived from NPC formation that occurs in dividing cells at the end of mitosis when the nuclear envelope (NE) and NPCs reform from disassembled precursors. However, NPC assembly also takes place during interphase into an intact NE. Importantly, this process is not restricted to dividing cells but also occurs during cell differentiation. Here, we will review aspects unique to this process, namely the regulation of nuclear expansion and the mechanisms of fusion between the outer and inner nuclear membranes. We will then discuss conserved and diverging mechanisms between post-mitotic and interphase assembly of the proteinaceous structure in light of recently published data.","lang":"eng"}],"date_updated":"2024-10-14T11:27:07Z","quality_controlled":"1","article_processing_charge":"No","date_created":"2022-04-07T07:53:12Z","month":"10","page":"469-477","publication_status":"published","language":[{"iso":"eng"}],"volume":119,"extern":"1","title":"Nuclear pore biogenesis into an intact nuclear envelope","publication_identifier":{"eissn":["1432-0886"],"issn":["0009-5915"]},"pmid":1,"type":"journal_article","doi":"10.1007/s00412-010-0289-2","publication":"Chromosoma","author":[{"full_name":"Doucet, Christine M.","last_name":"Doucet","first_name":"Christine M."},{"orcid":"0000-0002-2111-992X","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W"}],"scopus_import":"1"},{"author":[{"full_name":"Doucet, Christine M.","last_name":"Doucet","first_name":"Christine M."},{"last_name":"Talamas","full_name":"Talamas, Jessica A.","first_name":"Jessica A."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","full_name":"HETZER, Martin W","first_name":"Martin W","orcid":"0000-0002-2111-992X"}],"publication":"Cell","scopus_import":"1","extern":"1","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2010.04.036","open_access":"1"}],"doi":"10.1016/j.cell.2010.04.036","type":"journal_article","publication_identifier":{"issn":["0092-8674"]},"pmid":1,"oa":1,"title":"Cell cycle-dependent differences in nuclear pore complex assembly in metazoa","month":"06","volume":141,"language":[{"iso":"eng"}],"publication_status":"published","page":"1030-1041","quality_controlled":"1","date_created":"2022-04-07T07:53:29Z","article_processing_charge":"No","abstract":[{"lang":"eng","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."}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2024-10-14T11:28:00Z","fulldoi":"https://doi.org/10.1016/j.cell.2010.04.036","article_type":"original","keyword":["General Biochemistry","Genetics and Molecular Biology"],"date_published":"2010-06-11T00:00:00Z","year":"2010","citation":{"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>.","short":"C.M. Doucet, J.A. Talamas, M. Hetzer, Cell 141 (2010) 1030–1041.","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.","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>","ista":"Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041.","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>"},"publisher":"Elsevier","day":"11","oa_version":"Published Version","status":"public","_id":"11101","intvolume":"       141","external_id":{"pmid":["20550937"]},"issue":"6"},{"issue":"3","external_id":{"pmid":["20144761"]},"intvolume":"       140","day":"05","publisher":"Elsevier","year":"2010","citation":{"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>.","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>.","short":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, M. Hetzer, Cell 140 (2010) 372–383.","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>","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.","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.","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>"},"_id":"11102","status":"public","oa_version":"Published Version","date_published":"2010-02-05T00:00:00Z","keyword":["General Biochemistry","Genetics and Molecular Biology"],"article_type":"original","fulldoi":"https://doi.org/10.1016/j.cell.2009.12.054","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","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"}],"date_updated":"2024-10-14T11:28:14Z","quality_controlled":"1","article_processing_charge":"No","date_created":"2022-04-07T07:53:36Z","month":"02","page":"372-383","publication_status":"published","language":[{"iso":"eng"}],"volume":140,"extern":"1","title":"Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes","oa":1,"pmid":1,"publication_identifier":{"issn":["0092-8674"]},"type":"journal_article","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2009.12.054"}],"doi":"10.1016/j.cell.2009.12.054","publication":"Cell","author":[{"first_name":"Maya","full_name":"Capelson, Maya","last_name":"Capelson"},{"first_name":"Yun","full_name":"Liang, Yun","last_name":"Liang"},{"first_name":"Roberta","full_name":"Schulte, Roberta","last_name":"Schulte"},{"first_name":"William","full_name":"Mair, William","last_name":"Mair"},{"first_name":"Ulrich","last_name":"Wagner","full_name":"Wagner, Ulrich"},{"orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"}],"scopus_import":"1"},{"intvolume":"        17","external_id":{"pmid":["19922866"]},"issue":"5","oa_version":"Published Version","status":"public","_id":"11103","citation":{"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>","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.","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.","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>","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>.","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>."},"year":"2009","publisher":"Elsevier","day":"17","article_type":"review","fulldoi":"https://doi.org/10.1016/j.devcel.2009.10.007","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"date_published":"2009-11-17T00:00:00Z","date_updated":"2024-10-14T11:28:25Z","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."}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2022-04-07T07:53:45Z","article_processing_charge":"No","quality_controlled":"1","volume":17,"language":[{"iso":"eng"}],"publication_status":"published","page":"606-616","month":"11","doi":"10.1016/j.devcel.2009.10.007","main_file_link":[{"url":"https://doi.org/10.1016/j.devcel.2009.10.007","open_access":"1"}],"type":"journal_article","pmid":1,"publication_identifier":{"issn":["1534-5807"]},"oa":1,"title":"Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes","extern":"1","scopus_import":"1","author":[{"last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","first_name":"Martin W","orcid":"0000-0002-2111-992X"},{"full_name":"Wente, Susan R.","last_name":"Wente","first_name":"Susan R."}],"publication":"Developmental Cell"},{"type":"journal_article","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/embor.2009.147"}],"doi":"10.1038/embor.2009.147","title":"The role of nuclear pores in gene regulation, development and disease","oa":1,"pmid":1,"publication_identifier":{"eissn":["1469-3178"],"issn":["1469-221X"]},"extern":"1","scopus_import":"1","author":[{"last_name":"Capelson","full_name":"Capelson, Maya","first_name":"Maya"},{"last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W"}],"publication":"EMBO reports","article_processing_charge":"No","date_created":"2022-04-07T07:54:06Z","quality_controlled":"1","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/embor.2009.176"}]},"publication_status":"published","volume":10,"language":[{"iso":"eng"}],"page":"697-705","month":"07","keyword":["Genetics","Molecular Biology","Biochemistry"],"fulldoi":"https://doi.org/10.1038/embor.2009.147","article_type":"original","date_published":"2009-07-01T00:00:00Z","date_updated":"2024-10-14T11:28:35Z","abstract":[{"lang":"eng","text":"Nuclear-pore complexes (NPCs) are large protein channels that span the nuclear envelope (NE), which is a double membrane that encloses the nuclear genome of eukaryotes. Each of the typically 2,000–4,000 pores in the NE of vertebrate cells is composed of multiple copies of 30 different proteins known as nucleoporins. The evolutionarily conserved NPC proteins have the well-characterized function of mediating the transport of molecules between the nucleoplasm and the cytoplasm. Mutations in nucleoporins are often linked to specific developmental defects and disease, and the resulting phenotypes are usually interpreted as the consequences of perturbed nuclear transport activity. However, recent evidence suggests that NPCs have additional functions in chromatin organization and gene regulation, some of which might be independent of nuclear transport. Here, we review the transport-dependent and transport-independent roles of NPCs in the regulation of nuclear function and gene expression."}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","intvolume":"        10","issue":"7","external_id":{"pmid":["19543230"]},"oa_version":"Published Version","status":"public","_id":"11105","publisher":"EMBO","year":"2009","citation":{"ama":"Capelson M, Hetzer M. The role of nuclear pores in gene regulation, development and disease. <i>EMBO reports</i>. 2009;10(7):697-705. doi:<a href=\"https://doi.org/10.1038/embor.2009.147\">10.1038/embor.2009.147</a>","ista":"Capelson M, Hetzer M. 2009. The role of nuclear pores in gene regulation, development and disease. EMBO reports. 10(7), 697–705.","apa":"Capelson, M., &#38; Hetzer, M. (2009). The role of nuclear pores in gene regulation, development and disease. <i>EMBO Reports</i>. EMBO. <a href=\"https://doi.org/10.1038/embor.2009.147\">https://doi.org/10.1038/embor.2009.147</a>","ieee":"M. Capelson and M. Hetzer, “The role of nuclear pores in gene regulation, development and disease,” <i>EMBO reports</i>, vol. 10, no. 7. EMBO, pp. 697–705, 2009.","chicago":"Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation, Development and Disease.” <i>EMBO Reports</i>. EMBO, 2009. <a href=\"https://doi.org/10.1038/embor.2009.147\">https://doi.org/10.1038/embor.2009.147</a>.","mla":"Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation, Development and Disease.” <i>EMBO Reports</i>, vol. 10, no. 7, EMBO, 2009, pp. 697–705, doi:<a href=\"https://doi.org/10.1038/embor.2009.147\">10.1038/embor.2009.147</a>.","short":"M. Capelson, M. Hetzer, EMBO Reports 10 (2009) 697–705."},"day":"01"},{"month":"01","page":"284-295","publication_status":"published","volume":136,"language":[{"iso":"eng"}],"quality_controlled":"1","article_processing_charge":"No","date_created":"2022-04-07T07:54:52Z","publication":"Cell","author":[{"first_name":"Maximiliano A.","last_name":"D'Angelo","full_name":"D'Angelo, Maximiliano A."},{"full_name":"Raices, Marcela","last_name":"Raices","first_name":"Marcela"},{"first_name":"Siler H.","last_name":"Panowski","full_name":"Panowski, Siler H."},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"scopus_import":"1","extern":"1","title":"Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells","oa":1,"pmid":1,"publication_identifier":{"issn":["0092-8674"]},"type":"journal_article","doi":"10.1016/j.cell.2008.11.037","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2008.11.037","open_access":"1"}],"day":"23","publisher":"Elsevier","citation":{"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.","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>","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.","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>","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.","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>."},"year":"2009","_id":"11108","status":"public","oa_version":"Published Version","issue":"2","external_id":{"pmid":["19167330"]},"intvolume":"       136","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","abstract":[{"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.","lang":"eng"}],"date_updated":"2024-10-14T11:28:59Z","date_published":"2009-01-23T00:00:00Z","keyword":["General Biochemistry","Genetics and Molecular Biology"],"fulldoi":"https://doi.org/10.1016/j.cell.2008.11.037","article_type":"original"}]