[{"status":"public","intvolume":"         6","extern":"1","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"language":[{"iso":"eng"}],"citation":{"ama":"Ma P, Xue Y, Coquelle N, et al. Observing the overall rocking motion of a protein in a crystal. <i>Nature Communications</i>. 2015;6. doi:<a href=\"https://doi.org/10.1038/ncomms9361\">10.1038/ncomms9361</a>","apa":"Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., … Schanda, P. (2015). Observing the overall rocking motion of a protein in a crystal. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms9361\">https://doi.org/10.1038/ncomms9361</a>","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>.","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>.","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.","short":"P. Ma, Y. Xue, N. Coquelle, J.D. Haller, T. Yuwen, I. Ayala, O. Mikhailovskii, D. Willbold, J.-P. Colletier, N.R. Skrynnikov, P. Schanda, Nature Communications 6 (2015)."},"publication_status":"published","publication_identifier":{"issn":["2041-1723"]},"date_published":"2015-10-05T00:00:00Z","doi":"10.1038/ncomms9361","quality_controlled":"1","publisher":"Springer Nature","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2015","publication":"Nature Communications","_id":"8456","article_processing_charge":"No","article_type":"original","author":[{"full_name":"Ma, Peixiang","first_name":"Peixiang","last_name":"Ma"},{"last_name":"Xue","first_name":"Yi","full_name":"Xue, Yi"},{"first_name":"Nicolas","last_name":"Coquelle","full_name":"Coquelle, Nicolas"},{"first_name":"Jens D.","last_name":"Haller","full_name":"Haller, Jens D."},{"first_name":"Tairan","last_name":"Yuwen","full_name":"Yuwen, Tairan"},{"full_name":"Ayala, Isabel","first_name":"Isabel","last_name":"Ayala"},{"first_name":"Oleg","last_name":"Mikhailovskii","full_name":"Mikhailovskii, Oleg"},{"full_name":"Willbold, Dieter","first_name":"Dieter","last_name":"Willbold"},{"full_name":"Colletier, Jacques-Philippe","first_name":"Jacques-Philippe","last_name":"Colletier"},{"full_name":"Skrynnikov, Nikolai R.","first_name":"Nikolai R.","last_name":"Skrynnikov"},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda"}],"abstract":[{"text":"The large majority of three-dimensional structures of biological macromolecules have been determined by X-ray diffraction of crystalline samples. High-resolution structure determination crucially depends on the homogeneity of the protein crystal. Overall ‘rocking’ motion of molecules in the crystal is expected to influence diffraction quality, and such motion may therefore affect the process of solving crystal structures. Yet, so far overall molecular motion has not directly been observed in protein crystals, and the timescale of such dynamics remains unclear. Here we use solid-state NMR, X-ray diffraction methods and μs-long molecular dynamics simulations to directly characterize the rigid-body motion of a protein in different crystal forms. For ubiquitin crystals investigated in this study we determine the range of possible correlation times of rocking motion, 0.1–100 μs. The amplitude of rocking varies from one crystal form to another and is correlated with the resolution obtainable in X-ray diffraction experiments.","lang":"eng"}],"date_updated":"2021-01-12T08:19:24Z","day":"05","oa_version":"Published Version","month":"10","type":"journal_article","volume":6,"title":"Observing the overall rocking motion of a protein in a crystal","article_number":"8361","date_created":"2020-09-18T10:07:36Z"},{"author":[{"first_name":"P. M.","last_name":"Kraus","full_name":"Kraus, P. M."},{"full_name":"Tolstikhin, O. I.","first_name":"O. I.","last_name":"Tolstikhin"},{"last_name":"Baykusheva","first_name":"Denitsa Rangelova","full_name":"Baykusheva, Denitsa Rangelova","id":"71b4d059-2a03-11ee-914d-dfa3beed6530"},{"first_name":"A.","last_name":"Rupenyan","full_name":"Rupenyan, A."},{"full_name":"Schneider, J.","last_name":"Schneider","first_name":"J."},{"full_name":"Bisgaard, C. Z.","first_name":"C. Z.","last_name":"Bisgaard"},{"first_name":"T.","last_name":"Morishita","full_name":"Morishita, T."},{"full_name":"Jensen, F.","first_name":"F.","last_name":"Jensen"},{"full_name":"Madsen, L. B.","first_name":"L. B.","last_name":"Madsen"},{"first_name":"H. J.","last_name":"Wörner","full_name":"Wörner, H. J."}],"day":"05","article_number":"7039","title":"Observation of laser-induced electronic structure in oriented polyatomic molecules","publisher":"Springer Nature","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","pmid":1,"publication":"Nature Communications","article_type":"original","scopus_import":"1","article_processing_charge":"No","publication_identifier":{"eissn":["2041-1723"]},"doi":"10.1038/ncomms8039","quality_controlled":"1","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"language":[{"iso":"eng"}],"type":"journal_article","month":"05","oa_version":"Published Version","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"}],"date_updated":"2023-08-22T08:52:56Z","volume":6,"date_created":"2023-08-10T06:38:01Z","year":"2015","_id":"14016","oa":1,"publication_status":"published","date_published":"2015-05-05T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1038/ncomms8039","open_access":"1"}],"external_id":{"pmid":["25940229"]},"status":"public","extern":"1","intvolume":"         6","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>.","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.","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>","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>","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.","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>."}},{"date_published":"2014-02-27T00:00:00Z","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2014.02.004"}],"oa":1,"publication_status":"published","extern":"1","intvolume":"       156","citation":{"ista":"Buchwalter A, Hetzer M. 2014. Nuclear pores set the speed limit for mitosis. Cell. 156(5), 868–869.","mla":"Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit for Mitosis.” <i>Cell</i>, vol. 156, no. 5, Elsevier, 2014, pp. 868–69, doi:<a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">10.1016/j.cell.2014.02.004</a>.","apa":"Buchwalter, A., &#38; Hetzer, M. (2014). Nuclear pores set the speed limit for mitosis. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">https://doi.org/10.1016/j.cell.2014.02.004</a>","ama":"Buchwalter A, Hetzer M. Nuclear pores set the speed limit for mitosis. <i>Cell</i>. 2014;156(5):868-869. doi:<a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">10.1016/j.cell.2014.02.004</a>","short":"A. Buchwalter, M. Hetzer, Cell 156 (2014) 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.","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>."},"external_id":{"pmid":["24581486"]},"status":"public","volume":156,"date_created":"2022-04-07T07:50:04Z","page":"868-869","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."}],"date_updated":"2022-07-18T08:44:33Z","oa_version":"Published Version","type":"journal_article","month":"02","_id":"11080","year":"2014","doi":"10.1016/j.cell.2014.02.004","quality_controlled":"1","publication_identifier":{"issn":["0092-8674"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"issue":"5","title":"Nuclear pores set the speed limit for mitosis","author":[{"full_name":"Buchwalter, Abigail","first_name":"Abigail","last_name":"Buchwalter"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W"}],"day":"27","publication":"Cell","scopus_import":"1","article_processing_charge":"No","article_type":"original","publisher":"Elsevier","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","pmid":1},{"title":"Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics","author":[{"last_name":"Buchwalter","first_name":"Abigail L.","full_name":"Buchwalter, Abigail L."},{"full_name":"Liang, Yun","last_name":"Liang","first_name":"Yun"},{"full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","first_name":"Martin W","last_name":"HETZER"}],"day":"15","publication":"Molecular Biology of the Cell","article_type":"original","article_processing_charge":"No","scopus_import":"1","publisher":"American Society for Cell Biology","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","doi":"10.1091/mbc.e14-04-0865","quality_controlled":"1","publication_identifier":{"issn":["1059-1524","1939-4586"]},"keyword":["Cell Biology","Molecular Biology"],"issue":"16","language":[{"iso":"eng"}],"volume":25,"date_created":"2022-04-07T07:50:24Z","page":"2472-2484","type":"journal_article","month":"08","oa_version":"Published Version","date_updated":"2022-07-18T08:45:20Z","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."}],"_id":"11082","year":"2014","date_published":"2014-08-15T00:00:00Z","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1091/mbc.e14-04-0865"}],"publication_status":"published","oa":1,"extern":"1","intvolume":"        25","citation":{"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>","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.","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>.","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.","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>.","short":"A.L. Buchwalter, Y. Liang, M. Hetzer, Molecular Biology of the Cell 25 (2014) 2472–2484."},"status":"public"},{"publication_status":"published","date_published":"2014-08-01T00:00:00Z","status":"public","citation":{"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.","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.","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>.","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.","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>.","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>","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>"},"related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1093/bioinformatics/btz397"}]},"extern":"1","intvolume":"        30","oa_version":"None","month":"08","type":"journal_article","date_updated":"2021-01-12T08:19:25Z","abstract":[{"lang":"eng","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."}],"page":"2219-2220","date_created":"2020-09-18T10:08:07Z","volume":30,"year":"2014","_id":"8459","publication_identifier":{"issn":["1367-4803","1460-2059"]},"quality_controlled":"1","doi":"10.1093/bioinformatics/btu166","issue":"15","language":[{"iso":"eng"}],"keyword":["Statistics and Probability","Computational Theory and Mathematics","Biochemistry","Molecular Biology","Computational Mathematics","Computer Science Applications"],"day":"01","author":[{"last_name":"Morin","first_name":"Sébastien","full_name":"Morin, Sébastien"},{"first_name":"Troels E","last_name":"Linnet","full_name":"Linnet, Troels E"},{"full_name":"Lescanne, Mathilde","first_name":"Mathilde","last_name":"Lescanne"},{"last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"first_name":"Gary S","last_name":"Thompson","full_name":"Thompson, Gary S"},{"first_name":"Martin","last_name":"Tollinger","full_name":"Tollinger, Martin"},{"last_name":"Teilum","first_name":"Kaare","full_name":"Teilum, Kaare"},{"full_name":"Gagné, Stéphane","first_name":"Stéphane","last_name":"Gagné"},{"full_name":"Marion, Dominique","last_name":"Marion","first_name":"Dominique"},{"first_name":"Christian","last_name":"Griesinger","full_name":"Griesinger, Christian"},{"full_name":"Blackledge, Martin","last_name":"Blackledge","first_name":"Martin"},{"last_name":"d’Auvergne","first_name":"Edward J","full_name":"d’Auvergne, Edward J"}],"title":"Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data","publisher":"Oxford University Press","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_type":"original","article_processing_charge":"No","publication":"Bioinformatics"},{"publication":"Nature Communications","article_processing_charge":"No","scopus_import":"1","article_type":"original","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Springer Nature","pmid":1,"title":"Nanoporous frameworks exhibiting multiple stimuli responsiveness","article_number":"3588","author":[{"full_name":"Kundu, Pintu K.","first_name":"Pintu K.","last_name":"Kundu"},{"full_name":"Olsen, Gregory L.","first_name":"Gregory L.","last_name":"Olsen"},{"full_name":"Kiss, Vladimir","first_name":"Vladimir","last_name":"Kiss"},{"first_name":"Rafal","last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","full_name":"Klajn, Rafal"}],"day":"07","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"language":[{"iso":"eng"}],"doi":"10.1038/ncomms4588","quality_controlled":"1","publication_identifier":{"eissn":["2041-1723"]},"_id":"13402","year":"2014","volume":5,"date_created":"2023-08-01T09:46:27Z","date_updated":"2023-08-08T07:28:10Z","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."}],"month":"04","type":"journal_article","oa_version":"Published Version","intvolume":"         5","extern":"1","citation":{"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>.","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>","mla":"Kundu, Pintu K., et al. “Nanoporous Frameworks Exhibiting Multiple Stimuli Responsiveness.” <i>Nature Communications</i>, vol. 5, 3588, Springer Nature, 2014, doi:<a href=\"https://doi.org/10.1038/ncomms4588\">10.1038/ncomms4588</a>.","ista":"Kundu PK, Olsen GL, Kiss V, Klajn R. 2014. Nanoporous frameworks exhibiting multiple stimuli responsiveness. Nature Communications. 5, 3588.","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>"},"status":"public","external_id":{"pmid":["24709950"]},"date_published":"2014-04-07T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1038/ncomms4588","open_access":"1"}],"publication_status":"published","oa":1},{"date_published":"2013-01-01T00:00:00Z","publication_status":"published","citation":{"short":"B.H. Toyama, M. Hetzer, Nature Reviews Molecular Cell Biology 14 (2013) 55–61.","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.","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>.","ista":"Toyama BH, Hetzer M. 2013. Protein homeostasis: Live long, won’t prosper. Nature Reviews Molecular Cell Biology. 14, 55–61.","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>.","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>","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>"},"extern":"1","intvolume":"        14","external_id":{"pmid":["23258296"]},"status":"public","date_created":"2022-04-07T07:50:43Z","volume":14,"oa_version":"None","month":"01","type":"journal_article","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."}],"date_updated":"2022-07-18T08:37:53Z","page":"55-61","_id":"11084","year":"2013","quality_controlled":"1","doi":"10.1038/nrm3496","publication_identifier":{"issn":["1471-0072","1471-0080"]},"language":[{"iso":"eng"}],"keyword":["Cell Biology","Molecular Biology"],"title":"Protein homeostasis: Live long, won't prosper","day":"01","author":[{"first_name":"Brandon H.","last_name":"Toyama","full_name":"Toyama, Brandon H."},{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"}],"article_type":"original","article_processing_charge":"No","scopus_import":"1","publication":"Nature Reviews Molecular Cell Biology","pmid":1,"publisher":"Springer Nature","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd"},{"title":"Catastrophic nuclear envelope collapse in cancer cell micronuclei","author":[{"last_name":"Hatch","first_name":"Emily M.","full_name":"Hatch, Emily M."},{"first_name":"Andrew H.","last_name":"Fischer","full_name":"Fischer, Andrew H."},{"last_name":"Deerinck","first_name":"Thomas J.","full_name":"Deerinck, Thomas J."},{"orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W"}],"day":"03","publication":"Cell","article_processing_charge":"No","scopus_import":"1","article_type":"original","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publisher":"Elsevier","pmid":1,"doi":"10.1016/j.cell.2013.06.007","quality_controlled":"1","publication_identifier":{"issn":["0092-8674"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"issue":"1","volume":154,"date_created":"2022-04-07T07:50:51Z","page":"47-60","date_updated":"2022-07-18T08:45:47Z","abstract":[{"lang":"eng","text":"During mitotic exit, missegregated chromosomes can recruit their own nuclear envelope (NE) to form micronuclei (MN). MN have reduced functioning compared to primary nuclei in the same cell, although the two compartments appear to be structurally comparable. Here we show that over 60% of MN undergo an irreversible loss of compartmentalization during interphase due to NE collapse. This disruption of the MN, which is induced by defects in nuclear lamina assembly, drastically reduces nuclear functions and can trigger massive DNA damage. MN disruption is associated with chromatin compaction and invasion of endoplasmic reticulum (ER) tubules into the chromatin. We identified disrupted MN in both major subtypes of human non-small-cell lung cancer, suggesting that disrupted MN could be a useful objective biomarker for genomic instability in solid tumors. Our study shows that NE collapse is a key event underlying MN dysfunction and establishes a link between aberrant NE organization and aneuploidy."}],"month":"07","oa_version":"Published Version","type":"journal_article","_id":"11085","year":"2013","date_published":"2013-07-03T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2013.06.007","open_access":"1"}],"publication_status":"published","oa":1,"intvolume":"       154","extern":"1","citation":{"short":"E.M. Hatch, A.H. Fischer, T.J. Deerinck, M. Hetzer, Cell 154 (2013) 47–60.","chicago":"Hatch, Emily M., Andrew H. Fischer, Thomas J. Deerinck, and Martin Hetzer. “Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei.” <i>Cell</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">https://doi.org/10.1016/j.cell.2013.06.007</a>.","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>","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>.","ista":"Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. 2013. Catastrophic nuclear envelope collapse in cancer cell micronuclei. Cell. 154(1), 47–60.","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>"},"status":"public","external_id":{"pmid":["23827674"]}},{"publication_identifier":{"issn":["1553-7404"]},"doi":"10.1371/journal.pgen.1003308","quality_controlled":"1","keyword":["Cancer Research","Genetics (clinical)","Genetics","Molecular Biology","Ecology","Evolution","Behavior and Systematics"],"issue":"2","language":[{"iso":"eng"}],"author":[{"full_name":"Liang, Yun","first_name":"Yun","last_name":"Liang"},{"first_name":"Tobias M.","last_name":"Franks","full_name":"Franks, Tobias M."},{"last_name":"Marchetto","first_name":"Maria C.","full_name":"Marchetto, Maria C."},{"full_name":"Gage, Fred H.","last_name":"Gage","first_name":"Fred H."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W"}],"day":"28","article_number":"e1003308","title":"Dynamic association of NUP98 with the human genome","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publisher":"Public Library of Science","pmid":1,"publication":"PLoS Genetics","article_type":"original","scopus_import":"1","article_processing_charge":"No","publication_status":"published","oa":1,"date_published":"2013-02-28T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1371/journal.pgen.1003308","open_access":"1"}],"status":"public","external_id":{"pmid":["23468646"]},"intvolume":"         9","extern":"1","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>.","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.","short":"Y. Liang, T.M. Franks, M.C. Marchetto, F.H. Gage, M. Hetzer, PLoS Genetics 9 (2013).","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>","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>","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>.","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."},"oa_version":"Published Version","type":"journal_article","month":"02","date_updated":"2022-07-18T08:45:58Z","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."}],"volume":9,"date_created":"2022-04-07T07:50:59Z","year":"2013","_id":"11086"},{"year":"2013","_id":"11087","month":"08","type":"journal_article","oa_version":"Published Version","date_updated":"2022-07-18T08:50:47Z","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."}],"page":"971-982","date_created":"2022-04-07T07:51:08Z","volume":154,"status":"public","external_id":{"pmid":["23993091"]},"citation":{"short":"B.H. Toyama, J.N. Savas, S.K. Park, M.S. Harris, N.T. Ingolia, J.R. Yates, M. Hetzer, Cell 154 (2013) 971–982.","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>","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>.","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>"},"intvolume":"       154","extern":"1","oa":1,"publication_status":"published","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2013.07.037","open_access":"1"}],"date_published":"2013-08-29T00:00:00Z","pmid":1,"publisher":"Elsevier","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_type":"original","scopus_import":"1","article_processing_charge":"No","publication":"Cell","day":"29","author":[{"full_name":"Toyama, Brandon H.","first_name":"Brandon H.","last_name":"Toyama"},{"first_name":"Jeffrey N.","last_name":"Savas","full_name":"Savas, Jeffrey N."},{"full_name":"Park, Sung Kyu","last_name":"Park","first_name":"Sung Kyu"},{"first_name":"Michael S.","last_name":"Harris","full_name":"Harris, Michael S."},{"full_name":"Ingolia, Nicholas T.","last_name":"Ingolia","first_name":"Nicholas T."},{"full_name":"Yates, John R.","first_name":"John R.","last_name":"Yates"},{"last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"title":"Identification of long-lived proteins reveals exceptional stability of essential cellular structures","issue":"5","language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"publication_identifier":{"issn":["0092-8674"]},"quality_controlled":"1","doi":"10.1016/j.cell.2013.07.037"},{"year":"2013","user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","publisher":"Elsevier","article_type":"original","article_processing_charge":"No","_id":"8462","publication":"Journal of Molecular Biology","type":"journal_article","oa_version":"None","month":"08","abstract":[{"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.","lang":"eng"}],"day":"09","date_updated":"2022-08-25T14:56:24Z","page":"2722-2736","author":[{"full_name":"Rennella, E.","last_name":"Rennella","first_name":"E."},{"first_name":"T.","last_name":"Cutuil","full_name":"Cutuil, T."},{"first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"},{"first_name":"I.","last_name":"Ayala","full_name":"Ayala, I."},{"first_name":"F.","last_name":"Gabel","full_name":"Gabel, F."},{"last_name":"Forge","first_name":"V.","full_name":"Forge, V."},{"full_name":"Corazza, A.","last_name":"Corazza","first_name":"A."},{"full_name":"Esposito, G.","last_name":"Esposito","first_name":"G."},{"full_name":"Brutscher, B.","first_name":"B.","last_name":"Brutscher"}],"date_created":"2020-09-18T10:09:12Z","title":"Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure","volume":425,"status":"public","issue":"15","language":[{"iso":"eng"}],"citation":{"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>.","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.","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>","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>","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>.","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."},"keyword":["Molecular Biology"],"intvolume":"       425","extern":"1","publication_identifier":{"issn":["0022-2836"]},"publication_status":"published","quality_controlled":"1","date_published":"2013-08-09T00:00:00Z","doi":"10.1016/j.jmb.2013.04.028"},{"pmid":1,"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publisher":"Elsevier","article_processing_charge":"No","scopus_import":"1","article_type":"letter_note","publication":"Cell","day":"11","author":[{"first_name":"Emily M.","last_name":"Hatch","full_name":"Hatch, Emily M."},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W"}],"title":"RNP export by nuclear envelope budding","language":[{"iso":"eng"}],"issue":"4","keyword":["General Biochemistry","Genetics and Molecular Biology"],"publication_identifier":{"issn":["0092-8674"]},"quality_controlled":"1","doi":"10.1016/j.cell.2012.04.018","year":"2012","_id":"11090","date_updated":"2022-07-18T08:58:48Z","abstract":[{"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.","lang":"eng"}],"type":"journal_article","oa_version":"Published Version","month":"05","page":"733-735","date_created":"2022-04-07T07:51:45Z","volume":149,"status":"public","external_id":{"pmid":["22579277"]},"citation":{"ista":"Hatch EM, Hetzer M. 2012. RNP export by nuclear envelope budding. Cell. 149(4), 733–735.","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>.","apa":"Hatch, E. M., &#38; Hetzer, M. (2012). RNP export by nuclear envelope budding. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">https://doi.org/10.1016/j.cell.2012.04.018</a>","ama":"Hatch EM, Hetzer M. RNP export by nuclear envelope budding. <i>Cell</i>. 2012;149(4):733-735. doi:<a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">10.1016/j.cell.2012.04.018</a>","short":"E.M. Hatch, M. Hetzer, Cell 149 (2012) 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.","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>."},"extern":"1","intvolume":"       149","oa":1,"publication_status":"published","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2012.04.018"}],"date_published":"2012-05-11T00:00:00Z"},{"year":"2012","_id":"11093","page":"446-458","type":"journal_article","month":"01","oa_version":"Published Version","date_updated":"2022-07-18T08:53:16Z","abstract":[{"lang":"eng","text":"Nuclear pore complexes (NPCs) are built from ∼30 different proteins called nucleoporins or Nups. Previous studies have shown that several Nups exhibit cell-type-specific expression and that mutations in NPC components result in tissue-specific diseases. Here we show that a specific change in NPC composition is required for both myogenic and neuronal differentiation. The transmembrane nucleoporin Nup210 is absent in proliferating myoblasts and embryonic stem cells (ESCs) but becomes expressed and incorporated into NPCs during cell differentiation. Preventing Nup210 production by RNAi blocks myogenesis and the differentiation of ESCs into neuroprogenitors. We found that the addition of Nup210 to NPCs does not affect nuclear transport but is required for the induction of genes that are essential for cell differentiation. Our results identify a single change in NPC composition as an essential step in cell differentiation and establish a role for Nup210 in gene expression regulation and cell fate determination."}],"volume":22,"date_created":"2022-04-07T07:52:10Z","status":"public","external_id":{"pmid":["22264802"]},"extern":"1","intvolume":"        22","citation":{"short":"M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental Cell 22 (2012) 446–458.","chicago":"D’Angelo, Maximiliano A., J. Sebastian Gomez-Cavazos, Arianna Mei, Daniel H. Lackner, and Martin Hetzer. “A Change in Nuclear Pore Complex Composition Regulates Cell Differentiation.” <i>Developmental Cell</i>. Elsevier, 2012. <a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">https://doi.org/10.1016/j.devcel.2011.11.021</a>.","ieee":"M. A. D’Angelo, J. S. Gomez-Cavazos, A. Mei, D. H. Lackner, and M. Hetzer, “A change in nuclear pore complex composition regulates cell differentiation,” <i>Developmental Cell</i>, vol. 22, no. 2. Elsevier, pp. 446–458, 2012.","apa":"D’Angelo, M. A., Gomez-Cavazos, J. S., Mei, A., Lackner, D. H., &#38; Hetzer, M. (2012). A change in nuclear pore complex composition regulates cell differentiation. <i>Developmental Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">https://doi.org/10.1016/j.devcel.2011.11.021</a>","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>.","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>"},"oa":1,"publication_status":"published","date_published":"2012-01-19T00:00:00Z","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2011.11.021"}],"publisher":"Elsevier","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","pmid":1,"publication":"Developmental Cell","article_type":"original","scopus_import":"1","article_processing_charge":"No","author":[{"full_name":"D'Angelo, Maximiliano A.","last_name":"D'Angelo","first_name":"Maximiliano A."},{"full_name":"Gomez-Cavazos, J. Sebastian","first_name":"J. Sebastian","last_name":"Gomez-Cavazos"},{"full_name":"Mei, Arianna","first_name":"Arianna","last_name":"Mei"},{"first_name":"Daniel H.","last_name":"Lackner","full_name":"Lackner, Daniel H."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"day":"19","title":"A change in nuclear pore complex composition regulates cell differentiation","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"issue":"2","language":[{"iso":"eng"}],"publication_identifier":{"issn":["1534-5807"]},"doi":"10.1016/j.devcel.2011.11.021","quality_controlled":"1"},{"intvolume":"        75","extern":"1","citation":{"short":"M. Capelson, C. Doucet, M. Hetzer, Cold Spring Harbor Symposia on Quantitative Biology 75 (2011) 585–597.","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>.","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.","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>","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.","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>.","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>"},"external_id":{"pmid":["21502404"]},"status":"public","date_published":"2011-04-18T00:00:00Z","publication_status":"published","_id":"11100","year":"2011","volume":75,"date_created":"2022-04-07T07:53:18Z","page":"585-597","date_updated":"2022-07-18T08:54:23Z","abstract":[{"lang":"eng","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."}],"oa_version":"None","month":"04","type":"journal_article","keyword":["Genetics","Molecular Biology","Biochemistry"],"language":[{"iso":"eng"}],"doi":"10.1101/sqb.2010.75.059","quality_controlled":"1","publication_identifier":{"issn":["0091-7451","1943-4456"],"isbn":["9781936113071"]},"publication":"Cold Spring Harbor Symposia on Quantitative Biology","scopus_import":"1","article_processing_charge":"No","article_type":"original","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publisher":"Cold Spring Harbor Laboratory Press","pmid":1,"title":"Nuclear pore complexes: Guardians of the nuclear genome","author":[{"first_name":"M.","last_name":"Capelson","full_name":"Capelson, M."},{"last_name":"Doucet","first_name":"C.","full_name":"Doucet, C."},{"last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"day":"18"},{"title":"The nuclear envelope","day":"03","author":[{"first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"article_type":"original","scopus_import":"1","article_processing_charge":"No","publication":"Cold Spring Harbor Perspectives in Biology","pmid":1,"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publisher":"Cold Spring Harbor Laboratory","quality_controlled":"1","doi":"10.1101/cshperspect.a000539","publication_identifier":{"issn":["1943-0264"]},"issue":"3","language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"date_created":"2022-04-07T07:52:49Z","volume":2,"month":"02","type":"journal_article","oa_version":"None","date_updated":"2022-07-18T08:53:50Z","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"}],"page":"a000539-a000539","_id":"11097","year":"2010","date_published":"2010-02-03T00:00:00Z","publication_status":"published","citation":{"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>","ista":"Hetzer M. 2010. The nuclear envelope. Cold Spring Harbor Perspectives in Biology. 2(3), 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>.","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>","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.","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."},"intvolume":"         2","extern":"1","status":"public","external_id":{"pmid":["20300205"]}},{"author":[{"full_name":"Doucet, Christine M.","last_name":"Doucet","first_name":"Christine M."},{"first_name":"Jessica A.","last_name":"Talamas","full_name":"Talamas, Jessica A."},{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"}],"day":"11","title":"Cell cycle-dependent differences in nuclear pore complex assembly in metazoa","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publisher":"Elsevier","pmid":1,"publication":"Cell","article_type":"original","scopus_import":"1","article_processing_charge":"No","publication_identifier":{"issn":["0092-8674"]},"doi":"10.1016/j.cell.2010.04.036","quality_controlled":"1","keyword":["General Biochemistry","Genetics and Molecular Biology"],"issue":"6","language":[{"iso":"eng"}],"page":"1030-1041","type":"journal_article","oa_version":"Published Version","month":"06","date_updated":"2022-07-18T08:54:52Z","abstract":[{"text":"In metazoa, nuclear pore complexes (NPCs) assemble from disassembled precursors into a reforming nuclear envelope (NE) at the end of mitosis and into growing intact NEs during interphase. Here, we show via RNAi-mediated knockdown that ELYS, a nucleoporin critical for the recruitment of the essential Nup107/160 complex to chromatin, is required for NPC assembly at the end of mitosis but not during interphase. Conversely, the transmembrane nucleoporin POM121 is critical for the incorporation of the Nup107/160 complex into new assembly sites specifically during interphase. Strikingly, recruitment of the Nup107/160 complex to an intact NE involves a membrane curvature-sensing domain of its constituent Nup133, which is not required for postmitotic NPC formation. Our results suggest that in organisms with open mitosis, NPCs assemble via two distinct mechanisms to accommodate cell cycle-dependent differences in NE topology.","lang":"eng"}],"volume":141,"date_created":"2022-04-07T07:53:29Z","year":"2010","_id":"11101","oa":1,"publication_status":"published","date_published":"2010-06-11T00:00:00Z","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2010.04.036"}],"external_id":{"pmid":["20550937"]},"status":"public","intvolume":"       141","extern":"1","citation":{"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.","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>.","short":"C.M. Doucet, J.A. Talamas, M. Hetzer, Cell 141 (2010) 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>","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>.","ista":"Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041.","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>"}},{"pmid":1,"publisher":"Elsevier","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","scopus_import":"1","article_type":"original","publication":"Cell","day":"05","author":[{"first_name":"Maya","last_name":"Capelson","full_name":"Capelson, Maya"},{"first_name":"Yun","last_name":"Liang","full_name":"Liang, Yun"},{"full_name":"Schulte, Roberta","last_name":"Schulte","first_name":"Roberta"},{"last_name":"Mair","first_name":"William","full_name":"Mair, William"},{"first_name":"Ulrich","last_name":"Wagner","full_name":"Wagner, Ulrich"},{"orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W"}],"title":"Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes","language":[{"iso":"eng"}],"issue":"3","keyword":["General Biochemistry","Genetics and Molecular Biology"],"publication_identifier":{"issn":["0092-8674"]},"quality_controlled":"1","doi":"10.1016/j.cell.2009.12.054","year":"2010","_id":"11102","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":"2022-07-18T08:55:03Z","oa_version":"Published Version","type":"journal_article","month":"02","page":"372-383","date_created":"2022-04-07T07:53:36Z","volume":140,"status":"public","external_id":{"pmid":["20144761"]},"citation":{"short":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, M. Hetzer, Cell 140 (2010) 372–383.","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>.","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>","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>.","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.","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>"},"extern":"1","intvolume":"       140","publication_status":"published","oa":1,"main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2009.12.054","open_access":"1"}],"date_published":"2010-02-05T00:00:00Z"},{"article_type":"original","article_processing_charge":"No","_id":"8473","publication":"Journal of Biological Chemistry","year":"2010","publisher":"American Society for Biochemistry & Molecular Biology","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2020-09-18T10:11:23Z","title":"Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR","volume":285,"month":"02","oa_version":"None","type":"journal_article","day":"19","abstract":[{"text":"β2-microglobulin (β2m), the light chain of class I major histocompatibility complex, is responsible for the dialysis-related amyloidosis and, in patients undergoing long term dialysis, the full-length and chemically unmodified β2m converts into amyloid fibrils. The protein, belonging to the immunoglobulin superfamily, in common to other members of this family, experiences during its folding a long-lived intermediate associated to the trans-to-cis isomerization of Pro-32 that has been addressed as the precursor of the amyloid fibril formation. In this respect, previous studies on the W60G β2m mutant, showing that the lack of Trp-60 prevents fibril formation in mild aggregating condition, prompted us to reinvestigate the refolding kinetics of wild type and W60G β2m at atomic resolution by real-time NMR. The analysis, conducted at ambient temperature by the band selective flip angle short transient real-time two-dimensional NMR techniques and probing the β2m states every 15 s, revealed a more complex folding energy landscape than previously reported for wild type β2m, involving more than a single intermediate species, and shedding new light into the fibrillogenic pathway. Moreover, a significant difference in the kinetic scheme previously characterized by optical spectroscopic methods was discovered for the W60G β2m mutant.","lang":"eng"}],"date_updated":"2021-01-12T08:19:31Z","page":"5827-5835","author":[{"full_name":"Corazza, Alessandra","first_name":"Alessandra","last_name":"Corazza"},{"first_name":"Enrico","last_name":"Rennella","full_name":"Rennella, Enrico"},{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul"},{"full_name":"Mimmi, Maria Chiara","first_name":"Maria Chiara","last_name":"Mimmi"},{"full_name":"Cutuil, Thomas","first_name":"Thomas","last_name":"Cutuil"},{"last_name":"Raimondi","first_name":"Sara","full_name":"Raimondi, Sara"},{"full_name":"Giorgetti, Sofia","last_name":"Giorgetti","first_name":"Sofia"},{"full_name":"Fogolari, Federico","last_name":"Fogolari","first_name":"Federico"},{"full_name":"Viglino, Paolo","first_name":"Paolo","last_name":"Viglino"},{"full_name":"Frydman, Lucio","last_name":"Frydman","first_name":"Lucio"},{"full_name":"Gal, Maayan","first_name":"Maayan","last_name":"Gal"},{"first_name":"Vittorio","last_name":"Bellotti","full_name":"Bellotti, Vittorio"},{"full_name":"Brutscher, Bernhard","last_name":"Brutscher","first_name":"Bernhard"},{"full_name":"Esposito, Gennaro","first_name":"Gennaro","last_name":"Esposito"}],"issue":"8","language":[{"iso":"eng"}],"citation":{"ama":"Corazza A, Rennella E, Schanda P, et al. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. <i>Journal of Biological Chemistry</i>. 2010;285(8):5827-5835. doi:<a href=\"https://doi.org/10.1074/jbc.m109.061168\">10.1074/jbc.m109.061168</a>","apa":"Corazza, A., Rennella, E., Schanda, P., Mimmi, M. C., Cutuil, T., Raimondi, S., … Esposito, G. (2010). Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology. <a href=\"https://doi.org/10.1074/jbc.m109.061168\">https://doi.org/10.1074/jbc.m109.061168</a>","ista":"Corazza A, Rennella E, Schanda P, Mimmi MC, Cutuil T, Raimondi S, Giorgetti S, Fogolari F, Viglino P, Frydman L, Gal M, Bellotti V, Brutscher B, Esposito G. 2010. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. Journal of Biological Chemistry. 285(8), 5827–5835.","mla":"Corazza, Alessandra, et al. “Native-Unlike Long-Lived Intermediates along the Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin Revealed by Real-Time Two-Dimensional NMR.” <i>Journal of Biological Chemistry</i>, vol. 285, no. 8, American Society for Biochemistry &#38; Molecular Biology, 2010, pp. 5827–35, doi:<a href=\"https://doi.org/10.1074/jbc.m109.061168\">10.1074/jbc.m109.061168</a>.","chicago":"Corazza, Alessandra, Enrico Rennella, Paul Schanda, Maria Chiara Mimmi, Thomas Cutuil, Sara Raimondi, Sofia Giorgetti, et al. “Native-Unlike Long-Lived Intermediates along the Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin Revealed by Real-Time Two-Dimensional NMR.” <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology, 2010. <a href=\"https://doi.org/10.1074/jbc.m109.061168\">https://doi.org/10.1074/jbc.m109.061168</a>.","ieee":"A. Corazza <i>et al.</i>, “Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR,” <i>Journal of Biological Chemistry</i>, vol. 285, no. 8. American Society for Biochemistry &#38; Molecular Biology, pp. 5827–5835, 2010.","short":"A. Corazza, E. Rennella, P. Schanda, M.C. Mimmi, T. Cutuil, S. Raimondi, S. Giorgetti, F. Fogolari, P. Viglino, L. Frydman, M. Gal, V. Bellotti, B. Brutscher, G. Esposito, Journal of Biological Chemistry 285 (2010) 5827–5835."},"keyword":["Cell Biology","Biochemistry","Molecular Biology"],"intvolume":"       285","extern":"1","status":"public","quality_controlled":"1","doi":"10.1074/jbc.m109.061168","date_published":"2010-02-19T00:00:00Z","publication_identifier":{"issn":["0021-9258","1083-351X"]},"publication_status":"published"},{"department":[{"_id":"XiFe"}],"pmid":1,"publisher":"The Company of Biologists","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_type":"original","scopus_import":"1","article_processing_charge":"No","publication":"Development","day":"15","author":[{"last_name":"Feng","first_name":"Xiaoqi","id":"e0164712-22ee-11ed-b12a-d80fcdf35958","orcid":"0000-0002-4008-1234","full_name":"Feng, Xiaoqi"},{"full_name":"Dickinson, Hugh G.","first_name":"Hugh G.","last_name":"Dickinson"}],"title":"Tapetal cell fate, lineage and proliferation in the Arabidopsis anther","issue":"14","language":[{"iso":"eng"}],"keyword":["Developmental Biology","Molecular Biology","Anther Tapetum","Arabidopsis","Cell Fate Establishment","EMS1","Reproductive Cell Lineage"],"publication_identifier":{"issn":["1477-9129","0950-1991"]},"quality_controlled":"1","doi":"10.1242/dev.049320","year":"2010","acknowledgement":"We thank the following for providing mutant lines and reagents: Hong Ma, De Ye, Sacco De Vries, and Rod Scott for providing the pA9::Barnase lines and information on A9 expression patterns. Carla Galinha and Paolo Piazza gave valuable help with in situ hybridisation and qRT-PCR, respectively, and we acknowledge Qing Zhang, Helen Prescott and Matthew Dicks for providing excellent technical assistance. We are indebted to Miltos Tsiantis and Angela Hay for helpful discussion, and the research was funded by Oxford University through a Clarendon Scholarship to X.F., with additional financial support from Magdalen College (Oxford).","_id":"12199","month":"07","type":"journal_article","oa_version":"None","date_updated":"2023-05-08T10:57:11Z","abstract":[{"lang":"eng","text":"The four microsporangia of the flowering plant anther develop from archesporial cells in the L2 of the primordium. Within each microsporangium, developing microsporocytes are surrounded by concentric monolayers of tapetal, middle layer and endothecial cells. How this intricate array of tissues, each containing relatively few cells, is established in an organ possessing no formal meristems is poorly understood. We describe here the pivotal role of the LRR receptor kinase EXCESS MICROSPOROCYTES 1 (EMS1) in forming the monolayer of tapetal nurse cells in Arabidopsis. Unusually for plants, tapetal cells are specified very early in development, and are subsequently stimulated to proliferate by a receptor-like kinase (RLK) complex that includes EMS1. Mutations in members of this EMS1 signalling complex and its putative ligand result in male-sterile plants in which tapetal initials fail to proliferate. Surprisingly, these cells continue to develop, isolated at the locular periphery. Mutant and wild-type microsporangia expand at similar rates and the ‘tapetal’ space at the periphery of mutant locules becomes occupied by microsporocytes. However, induction of late expression of EMS1 in the few tapetal initials in ems1 plants results in their proliferation to generate a functional tapetum, and this proliferation suppresses microsporocyte number. Our experiments also show that integrity of the tapetal monolayer is crucial for the maintenance of the polarity of divisions within it. This unexpected autonomy of the tapetal ‘lineage’ is discussed in the context of tissue development in complex plant organs, where constancy in size, shape and cell number is crucial."}],"page":"2409-2416","date_created":"2023-01-16T09:21:54Z","volume":137,"status":"public","external_id":{"pmid":["20570940"]},"citation":{"apa":"Feng, X., &#38; Dickinson, H. G. (2010). Tapetal cell fate, lineage and proliferation in the Arabidopsis anther. <i>Development</i>. The Company of Biologists. <a href=\"https://doi.org/10.1242/dev.049320\">https://doi.org/10.1242/dev.049320</a>","ista":"Feng X, Dickinson HG. 2010. Tapetal cell fate, lineage and proliferation in the Arabidopsis anther. Development. 137(14), 2409–2416.","mla":"Feng, Xiaoqi, and Hugh G. Dickinson. “Tapetal Cell Fate, Lineage and Proliferation in the Arabidopsis Anther.” <i>Development</i>, vol. 137, no. 14, The Company of Biologists, 2010, pp. 2409–16, doi:<a href=\"https://doi.org/10.1242/dev.049320\">10.1242/dev.049320</a>.","ama":"Feng X, Dickinson HG. Tapetal cell fate, lineage and proliferation in the Arabidopsis anther. <i>Development</i>. 2010;137(14):2409-2416. doi:<a href=\"https://doi.org/10.1242/dev.049320\">10.1242/dev.049320</a>","short":"X. Feng, H.G. Dickinson, Development 137 (2010) 2409–2416.","chicago":"Feng, Xiaoqi, and Hugh G. Dickinson. “Tapetal Cell Fate, Lineage and Proliferation in the Arabidopsis Anther.” <i>Development</i>. The Company of Biologists, 2010. <a href=\"https://doi.org/10.1242/dev.049320\">https://doi.org/10.1242/dev.049320</a>.","ieee":"X. Feng and H. G. Dickinson, “Tapetal cell fate, lineage and proliferation in the Arabidopsis anther,” <i>Development</i>, vol. 137, no. 14. The Company of Biologists, pp. 2409–2416, 2010."},"intvolume":"       137","extern":"1","publication_status":"published","date_published":"2010-07-15T00:00:00Z"},{"page":"606-616","date_updated":"2022-07-18T08:55:01Z","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."}],"month":"11","oa_version":"Published Version","type":"journal_article","volume":17,"date_created":"2022-04-07T07:53:45Z","year":"2009","_id":"11103","oa":1,"publication_status":"published","date_published":"2009-11-17T00:00:00Z","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2009.10.007"}],"external_id":{"pmid":["19922866"]},"status":"public","intvolume":"        17","extern":"1","citation":{"short":"M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.","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.","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>.","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.","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>.","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>","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>"},"author":[{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"first_name":"Susan R.","last_name":"Wente","full_name":"Wente, Susan R."}],"day":"17","title":"Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publisher":"Elsevier","pmid":1,"publication":"Developmental Cell","article_processing_charge":"No","scopus_import":"1","article_type":"review","publication_identifier":{"issn":["1534-5807"]},"doi":"10.1016/j.devcel.2009.10.007","quality_controlled":"1","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"language":[{"iso":"eng"}],"issue":"5"}]