[{"date_published":"2013-07-03T00:00:00Z","type":"journal_article","oa":1,"publication_identifier":{"issn":["0092-8674"]},"status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2013.06.007"}],"publication":"Cell","month":"07","oa_version":"Published Version","language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"external_id":{"pmid":["23827674"]},"date_updated":"2022-07-18T08:45:47Z","citation":{"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>","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.","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>.","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>.","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","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"}],"doi":"10.1016/j.cell.2013.06.007","day":"03","extern":"1","volume":154,"author":[{"last_name":"Hatch","first_name":"Emily M.","full_name":"Hatch, Emily M."},{"full_name":"Fischer, Andrew H.","first_name":"Andrew H.","last_name":"Fischer"},{"full_name":"Deerinck, Thomas J.","last_name":"Deerinck","first_name":"Thomas J."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"issue":"1","pmid":1,"_id":"11085","scopus_import":"1","title":"Catastrophic nuclear envelope collapse in cancer cell micronuclei","intvolume":"       154","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:50:51Z","page":"47-60","quality_controlled":"1","article_type":"original","publisher":"Elsevier"},{"publication":"Cell","oa_version":"Published Version","month":"08","language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"date_published":"2013-08-29T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["0092-8674"]},"oa":1,"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2013.07.037"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","_id":"11087","pmid":1,"scopus_import":"1","author":[{"last_name":"Toyama","first_name":"Brandon H.","full_name":"Toyama, Brandon H."},{"first_name":"Jeffrey N.","last_name":"Savas","full_name":"Savas, Jeffrey N."},{"full_name":"Park, Sung Kyu","last_name":"Park","first_name":"Sung Kyu"},{"full_name":"Harris, Michael S.","first_name":"Michael S.","last_name":"Harris"},{"full_name":"Ingolia, Nicholas T.","first_name":"Nicholas T.","last_name":"Ingolia"},{"full_name":"Yates, John R.","last_name":"Yates","first_name":"John R."},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"issue":"5","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:51:08Z","title":"Identification of long-lived proteins reveals exceptional stability of essential cellular structures","intvolume":"       154","page":"971-982","quality_controlled":"1","publisher":"Elsevier","article_type":"original","date_updated":"2022-07-18T08:50:47Z","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.","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>","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>","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."},"year":"2013","external_id":{"pmid":["23993091"]},"doi":"10.1016/j.cell.2013.07.037","day":"29","abstract":[{"text":"Intracellular proteins with long lifespans have recently been linked to age-dependent defects, ranging from decreased fertility to the functional decline of neurons. Why long-lived proteins exist in metabolically active cellular environments and how they are maintained over time remains poorly understood. Here, we provide a system-wide identification of proteins with exceptional lifespans in the rat brain. These proteins are inefficiently replenished despite being translated robustly throughout adulthood. Using nucleoporins as a paradigm for long-term protein persistence, we found that nuclear pore complexes (NPCs) are maintained over a cell’s life through slow but finite exchange of even its most stable subcomplexes. This maintenance is limited, however, as some nucleoporin levels decrease during aging, providing a rationale for the previously observed age-dependent deterioration of NPC function. Our identification of a long-lived proteome reveals cellular components that are at increased risk for damage accumulation, linking long-term protein persistence to the cellular aging process.","lang":"eng"}],"volume":154,"extern":"1"},{"article_type":"original","publisher":"Springer Nature","keyword":["Spectroscopy","Biochemistry"],"language":[{"iso":"eng"}],"quality_controlled":"1","page":"263-280","intvolume":"        57","title":"Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin","month":"10","date_created":"2020-09-18T10:09:05Z","article_processing_charge":"No","publication_status":"published","oa_version":"None","issue":"3","author":[{"full_name":"Haller, Jens D.","first_name":"Jens D.","last_name":"Haller"},{"first_name":"Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"_id":"8461","publication":"Journal of Biomolecular NMR","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","extern":"1","volume":57,"abstract":[{"text":"Solid-state NMR provides insight into protein motion over time scales ranging from picoseconds to seconds. While in solution state the methodology to measure protein dynamics is well established, there is currently no such consensus protocol for measuring dynamics in solids. In this article, we perform a detailed investigation of measurement protocols for fast motions, i.e. motions ranging from picoseconds to a few microseconds, which is the range covered by dipolar coupling and relaxation experiments. We perform a detailed theoretical investigation how dipolar couplings and relaxation data can provide information about amplitudes and time scales of local motion. We show that the measurement of dipolar couplings is crucial for obtaining accurate motional parameters, while systematic errors are found when only relaxation data are used. Based on this realization, we investigate how the REDOR experiment can provide such data in a very accurate manner. We identify that with accurate rf calibration, and explicit consideration of rf field inhomogeneities, one can obtain highly accurate absolute order parameters. We then perform joint model-free analyses of 6 relaxation data sets and dipolar couplings, based on previously existing, as well as new data sets on microcrystalline ubiquitin. We show that nanosecond motion can be detected primarily in loop regions, and compare solid-state data to solution-state relaxation and RDC analyses. The protocols investigated here will serve as a useful basis towards the establishment of a routine protocol for the characterization of ps–μs motions in proteins by solid-state NMR.","lang":"eng"}],"day":"09","publication_identifier":{"issn":["0925-2738","1573-5001"]},"doi":"10.1007/s10858-013-9787-x","type":"journal_article","date_published":"2013-10-09T00:00:00Z","year":"2013","citation":{"apa":"Haller, J. D., &#38; Schanda, P. (2013). Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin. <i>Journal of Biomolecular NMR</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s10858-013-9787-x\">https://doi.org/10.1007/s10858-013-9787-x</a>","ama":"Haller JD, Schanda P. Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin. <i>Journal of Biomolecular NMR</i>. 2013;57(3):263-280. doi:<a href=\"https://doi.org/10.1007/s10858-013-9787-x\">10.1007/s10858-013-9787-x</a>","ieee":"J. D. Haller and P. Schanda, “Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin,” <i>Journal of Biomolecular NMR</i>, vol. 57, no. 3. Springer Nature, pp. 263–280, 2013.","chicago":"Haller, Jens D., and Paul Schanda. “Amplitudes and Time Scales of Picosecond-to-Microsecond Motion in Proteins Studied by Solid-State NMR: A Critical Evaluation of Experimental Approaches and Application to Crystalline Ubiquitin.” <i>Journal of Biomolecular NMR</i>. Springer Nature, 2013. <a href=\"https://doi.org/10.1007/s10858-013-9787-x\">https://doi.org/10.1007/s10858-013-9787-x</a>.","mla":"Haller, Jens D., and Paul Schanda. “Amplitudes and Time Scales of Picosecond-to-Microsecond Motion in Proteins Studied by Solid-State NMR: A Critical Evaluation of Experimental Approaches and Application to Crystalline Ubiquitin.” <i>Journal of Biomolecular NMR</i>, vol. 57, no. 3, Springer Nature, 2013, pp. 263–80, doi:<a href=\"https://doi.org/10.1007/s10858-013-9787-x\">10.1007/s10858-013-9787-x</a>.","short":"J.D. Haller, P. Schanda, Journal of Biomolecular NMR 57 (2013) 263–280.","ista":"Haller JD, Schanda P. 2013. Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin. Journal of Biomolecular NMR. 57(3), 263–280."},"date_updated":"2021-01-12T08:19:26Z"},{"publication":"Journal of the American Chemical Society","month":"10","oa_version":"Preprint","keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"language":[{"iso":"eng"}],"type":"journal_article","date_published":"2013-10-30T00:00:00Z","oa":1,"publication_identifier":{"eissn":["15205126"],"issn":["00027863"]},"status":"public","user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","main_file_link":[{"open_access":"1","url":"https://arxiv.org/abs/1310.5724"}],"issue":"43","author":[{"id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d","first_name":"Jérémie A","last_name":"Palacci","orcid":"0000-0002-7253-9465","full_name":"Palacci, Jérémie A"},{"full_name":"Sacanna, Stefano","last_name":"Sacanna","first_name":"Stefano"},{"full_name":"Vatchinsky, Adrian","first_name":"Adrian","last_name":"Vatchinsky"},{"full_name":"Chaikin, Paul M.","last_name":"Chaikin","first_name":"Paul M."},{"full_name":"Pine, David J.","last_name":"Pine","first_name":"David J."}],"scopus_import":"1","pmid":1,"_id":"9167","intvolume":"       135","title":"Photoactivated colloidal dockers for cargo transportation","article_processing_charge":"No","date_created":"2021-02-18T14:31:26Z","publication_status":"published","quality_controlled":"1","page":"15978-15981","article_type":"original","publisher":"American Chemical Society","external_id":{"pmid":["24131488"],"arxiv":["1310.5724"]},"citation":{"mla":"Palacci, Jérémie A., et al. “Photoactivated Colloidal Dockers for Cargo Transportation.” <i>Journal of the American Chemical Society</i>, vol. 135, no. 43, American Chemical Society, 2013, pp. 15978–81, doi:<a href=\"https://doi.org/10.1021/ja406090s\">10.1021/ja406090s</a>.","short":"J.A. Palacci, S. Sacanna, A. Vatchinsky, P.M. Chaikin, D.J. Pine, Journal of the American Chemical Society 135 (2013) 15978–15981.","ista":"Palacci JA, Sacanna S, Vatchinsky A, Chaikin PM, Pine DJ. 2013. Photoactivated colloidal dockers for cargo transportation. Journal of the American Chemical Society. 135(43), 15978–15981.","ama":"Palacci JA, Sacanna S, Vatchinsky A, Chaikin PM, Pine DJ. Photoactivated colloidal dockers for cargo transportation. <i>Journal of the American Chemical Society</i>. 2013;135(43):15978-15981. doi:<a href=\"https://doi.org/10.1021/ja406090s\">10.1021/ja406090s</a>","apa":"Palacci, J. A., Sacanna, S., Vatchinsky, A., Chaikin, P. M., &#38; Pine, D. J. (2013). Photoactivated colloidal dockers for cargo transportation. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja406090s\">https://doi.org/10.1021/ja406090s</a>","ieee":"J. A. Palacci, S. Sacanna, A. Vatchinsky, P. M. Chaikin, and D. J. Pine, “Photoactivated colloidal dockers for cargo transportation,” <i>Journal of the American Chemical Society</i>, vol. 135, no. 43. American Chemical Society, pp. 15978–15981, 2013.","chicago":"Palacci, Jérémie A, Stefano Sacanna, Adrian Vatchinsky, Paul M. Chaikin, and David J. Pine. “Photoactivated Colloidal Dockers for Cargo Transportation.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2013. <a href=\"https://doi.org/10.1021/ja406090s\">https://doi.org/10.1021/ja406090s</a>."},"year":"2013","date_updated":"2021-02-22T10:10:41Z","abstract":[{"lang":"eng","text":"We introduce a self-propelled colloidal hematite docker that can be steered to a small particle cargo many times its size, dock, transport the cargo to a remote location, and then release it. The self-propulsion and docking are reversible and activated by visible light. The docker can be steered either by a weak uniform magnetic field or by nanoscale tracks in a textured substrate. The light-activated motion and docking originate from osmotic/phoretic particle transport in a concentration gradient of fuel, hydrogen peroxide, induced by the photocatalytic activity of the hematite. The docking mechanism is versatile and can be applied to various materials and shapes. The hematite dockers are simple single-component particles and are synthesized in bulk quantities. This system opens up new possibilities for designing complex micrometer-size factories as well as new biomimetic systems."}],"day":"30","doi":"10.1021/ja406090s","arxiv":1,"extern":"1","volume":135},{"publication_identifier":{"issn":["0092-8674"]},"oa":1,"type":"journal_article","date_published":"2012-05-11T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2012.04.018","open_access":"1"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","oa_version":"Published Version","month":"05","publication":"Cell","keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"day":"11","doi":"10.1016/j.cell.2012.04.018","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."}],"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>.","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>.","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>","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>"},"year":"2012","date_updated":"2022-07-18T08:58:48Z","external_id":{"pmid":["22579277"]},"volume":149,"extern":"1","article_processing_charge":"No","date_created":"2022-04-07T07:51:45Z","publication_status":"published","intvolume":"       149","title":"RNP export by nuclear envelope budding","scopus_import":"1","_id":"11090","pmid":1,"issue":"4","author":[{"full_name":"Hatch, Emily M.","last_name":"Hatch","first_name":"Emily M."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"publisher":"Elsevier","article_type":"letter_note","quality_controlled":"1","page":"733-735"},{"oa_version":"Published Version","month":"01","publication":"Developmental Cell","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["1534-5807"]},"oa":1,"type":"journal_article","date_published":"2012-01-19T00:00:00Z","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2011.11.021"}],"status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","date_created":"2022-04-07T07:52:10Z","article_processing_charge":"No","publication_status":"published","intvolume":"        22","title":"A change in nuclear pore complex composition regulates cell differentiation","scopus_import":"1","pmid":1,"_id":"11093","issue":"2","author":[{"first_name":"Maximiliano A.","last_name":"D'Angelo","full_name":"D'Angelo, Maximiliano A."},{"full_name":"Gomez-Cavazos, J. Sebastian","last_name":"Gomez-Cavazos","first_name":"J. Sebastian"},{"first_name":"Arianna","last_name":"Mei","full_name":"Mei, Arianna"},{"last_name":"Lackner","first_name":"Daniel H.","full_name":"Lackner, Daniel H."},{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"publisher":"Elsevier","article_type":"original","quality_controlled":"1","page":"446-458","day":"19","doi":"10.1016/j.devcel.2011.11.021","abstract":[{"text":"Nuclear pore complexes (NPCs) are built from ∼30 different proteins called nucleoporins or Nups. Previous studies have shown that several Nups exhibit cell-type-specific expression and that mutations in NPC components result in tissue-specific diseases. Here we show that a specific change in NPC composition is required for both myogenic and neuronal differentiation. The transmembrane nucleoporin Nup210 is absent in proliferating myoblasts and embryonic stem cells (ESCs) but becomes expressed and incorporated into NPCs during cell differentiation. Preventing Nup210 production by RNAi blocks myogenesis and the differentiation of ESCs into neuroprogenitors. We found that the addition of Nup210 to NPCs does not affect nuclear transport but is required for the induction of genes that are essential for cell differentiation. Our results identify a single change in NPC composition as an essential step in cell differentiation and establish a role for Nup210 in gene expression regulation and cell fate determination.","lang":"eng"}],"citation":{"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>.","apa":"D’Angelo, M. A., Gomez-Cavazos, J. S., Mei, A., Lackner, D. H., &#38; Hetzer, M. (2012). A change in nuclear pore complex composition regulates cell differentiation. <i>Developmental Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">https://doi.org/10.1016/j.devcel.2011.11.021</a>","ama":"D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. A change in nuclear pore complex composition regulates cell differentiation. <i>Developmental Cell</i>. 2012;22(2):446-458. doi:<a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">10.1016/j.devcel.2011.11.021</a>","ista":"D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. 2012. A change in nuclear pore complex composition regulates cell differentiation. Developmental Cell. 22(2), 446–458.","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","date_updated":"2022-07-18T08:53:16Z","external_id":{"pmid":["22264802"]},"volume":22,"extern":"1"},{"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"language":[{"iso":"eng"}],"publication":"Journal of the American Chemical Society","month":"11","oa_version":"Published Version","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","type":"journal_article","date_published":"2012-11-26T00:00:00Z","publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"quality_controlled":"1","page":"19564-19567","article_type":"original","publisher":"American Chemical Society","issue":"48","author":[{"first_name":"Olga","last_name":"Chovnik","full_name":"Chovnik, Olga"},{"full_name":"Balgley, Renata","first_name":"Renata","last_name":"Balgley"},{"full_name":"Goldman, Joel R.","first_name":"Joel R.","last_name":"Goldman"},{"full_name":"Klajn, Rafal","first_name":"Rafal","last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"scopus_import":"1","_id":"13407","pmid":1,"intvolume":"       134","title":"Dynamically self-assembling carriers enable guiding of diamagnetic particles by weak magnets","article_processing_charge":"No","date_created":"2023-08-01T09:47:42Z","publication_status":"published","extern":"1","volume":134,"external_id":{"pmid":["23181449"]},"citation":{"ama":"Chovnik O, Balgley R, Goldman JR, Klajn R. Dynamically self-assembling carriers enable guiding of diamagnetic particles by weak magnets. <i>Journal of the American Chemical Society</i>. 2012;134(48):19564-19567. doi:<a href=\"https://doi.org/10.1021/ja309633v\">10.1021/ja309633v</a>","apa":"Chovnik, O., Balgley, R., Goldman, J. R., &#38; Klajn, R. (2012). Dynamically self-assembling carriers enable guiding of diamagnetic particles by weak magnets. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja309633v\">https://doi.org/10.1021/ja309633v</a>","ieee":"O. Chovnik, R. Balgley, J. R. Goldman, and R. Klajn, “Dynamically self-assembling carriers enable guiding of diamagnetic particles by weak magnets,” <i>Journal of the American Chemical Society</i>, vol. 134, no. 48. American Chemical Society, pp. 19564–19567, 2012.","chicago":"Chovnik, Olga, Renata Balgley, Joel R. Goldman, and Rafal Klajn. “Dynamically Self-Assembling Carriers Enable Guiding of Diamagnetic Particles by Weak Magnets.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2012. <a href=\"https://doi.org/10.1021/ja309633v\">https://doi.org/10.1021/ja309633v</a>.","mla":"Chovnik, Olga, et al. “Dynamically Self-Assembling Carriers Enable Guiding of Diamagnetic Particles by Weak Magnets.” <i>Journal of the American Chemical Society</i>, vol. 134, no. 48, American Chemical Society, 2012, pp. 19564–67, doi:<a href=\"https://doi.org/10.1021/ja309633v\">10.1021/ja309633v</a>.","short":"O. Chovnik, R. Balgley, J.R. Goldman, R. Klajn, Journal of the American Chemical Society 134 (2012) 19564–19567.","ista":"Chovnik O, Balgley R, Goldman JR, Klajn R. 2012. Dynamically self-assembling carriers enable guiding of diamagnetic particles by weak magnets. Journal of the American Chemical Society. 134(48), 19564–19567."},"year":"2012","date_updated":"2023-08-08T07:51:10Z","abstract":[{"text":"We show that diamagnetic particles can be remotely manipulated by a magnet by the reversible adsorption of dual-responsive, light-switchable/superparamagnetic nanoparticles down to their surface. Adsorption occurs upon exposure to UV light, and can be reversed thermally or by ambient light. The dynamic self-assembly of thin films of the dual-responsive nanoparticles induces attractive interactions between diamagnetic particles. We demonstrate that catalytic amounts of the dual-responsive nanoparticles are sufficient to magnetically guide and deliver the diamagnetic particles to desired locations, where they can then be released by disassembling the dynamic layers of superparamagnetic nanoparticles with visible light.","lang":"eng"}],"day":"26","doi":"10.1021/ja309633v"},{"type":"journal_article","date_published":"2011-04-18T00:00:00Z","publication_identifier":{"isbn":["9781936113071"],"issn":["0091-7451","1943-4456"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","publication":"Cold Spring Harbor Symposia on Quantitative Biology","month":"04","oa_version":"None","keyword":["Genetics","Molecular Biology","Biochemistry"],"language":[{"iso":"eng"}],"external_id":{"pmid":["21502404"]},"citation":{"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>","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>","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.","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.","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."},"year":"2011","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."}],"day":"18","doi":"10.1101/sqb.2010.75.059","extern":"1","volume":75,"author":[{"full_name":"Capelson, M.","last_name":"Capelson","first_name":"M."},{"full_name":"Doucet, C.","last_name":"Doucet","first_name":"C."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"scopus_import":"1","pmid":1,"_id":"11100","intvolume":"        75","title":"Nuclear pore complexes: Guardians of the nuclear genome","date_created":"2022-04-07T07:53:18Z","article_processing_charge":"No","publication_status":"published","quality_controlled":"1","page":"585-597","article_type":"original","publisher":"Cold Spring Harbor Laboratory Press"},{"volume":210,"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","year":"2011","citation":{"apa":"Schanda, P., Meier, B. H., &#38; Ernst, M. (2011). Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR. <i>Journal of Magnetic Resonance</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmr.2011.03.015\">https://doi.org/10.1016/j.jmr.2011.03.015</a>","ama":"Schanda P, Meier BH, Ernst M. Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR. <i>Journal of Magnetic Resonance</i>. 2011;210(2):246-259. doi:<a href=\"https://doi.org/10.1016/j.jmr.2011.03.015\">10.1016/j.jmr.2011.03.015</a>","chicago":"Schanda, Paul, Beat H. Meier, and Matthias Ernst. “Accurate Measurement of One-Bond H–X Heteronuclear Dipolar Couplings in MAS Solid-State NMR.” <i>Journal of Magnetic Resonance</i>. Elsevier, 2011. <a href=\"https://doi.org/10.1016/j.jmr.2011.03.015\">https://doi.org/10.1016/j.jmr.2011.03.015</a>.","ieee":"P. Schanda, B. H. Meier, and M. Ernst, “Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR,” <i>Journal of Magnetic Resonance</i>, vol. 210, no. 2. Elsevier, pp. 246–259, 2011.","mla":"Schanda, Paul, et al. “Accurate Measurement of One-Bond H–X Heteronuclear Dipolar Couplings in MAS Solid-State NMR.” <i>Journal of Magnetic Resonance</i>, vol. 210, no. 2, Elsevier, 2011, pp. 246–59, doi:<a href=\"https://doi.org/10.1016/j.jmr.2011.03.015\">10.1016/j.jmr.2011.03.015</a>.","short":"P. Schanda, B.H. Meier, M. Ernst, Journal of Magnetic Resonance 210 (2011) 246–259.","ista":"Schanda P, Meier BH, Ernst M. 2011. Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR. Journal of Magnetic Resonance. 210(2), 246–259."},"date_updated":"2021-01-12T08:19:29Z","type":"journal_article","date_published":"2011-06-01T00:00:00Z","publication_identifier":{"issn":["1090-7807"]},"day":"01","doi":"10.1016/j.jmr.2011.03.015","abstract":[{"lang":"eng","text":"The accurate experimental determination of dipolar-coupling constants for one-bond heteronuclear dipolar couplings in solids is a key for the quantification of the amplitudes of motional processes. Averaging of the dipolar coupling reports on motions on time scales up to the inverse of the coupling constant, in our case tens of microseconds. Combining dipolar-coupling derived order parameters that characterize the amplitudes of the motion with relaxation data leads to a more precise characterization of the dynamical parameters and helps to disentangle the amplitudes and the time scales of the motional processes, which impact relaxation rates in a highly correlated way. Here. we describe and characterize an improved experimental protocol – based on REDOR – to measure these couplings in perdeuterated proteins with a reduced sensitivity to experimental missettings. Because such effects are presently the dominant source of systematic errors in experimental dipolar-coupling measurements, these compensated experiments should help to significantly improve the precision of such data. A detailed comparison with other commonly used pulse sequences (T-MREV, phase-inverted CP,R18 5/2, and R18 7/1) is provided."}],"quality_controlled":"1","page":"246-259","keyword":["Nuclear and High Energy Physics","Biophysics","Biochemistry","Condensed Matter Physics"],"language":[{"iso":"eng"}],"publisher":"Elsevier","article_type":"original","_id":"8469","publication":"Journal of Magnetic Resonance","issue":"2","author":[{"last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"full_name":"Meier, Beat H.","last_name":"Meier","first_name":"Beat H."},{"full_name":"Ernst, Matthias","last_name":"Ernst","first_name":"Matthias"}],"date_created":"2020-09-18T10:10:50Z","article_processing_charge":"No","publication_status":"published","oa_version":"None","intvolume":"       210","title":"Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR","month":"06"},{"type":"journal_article","date_published":"2010-02-03T00:00:00Z","publication_identifier":{"issn":["1943-0264"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","publication":"Cold Spring Harbor Perspectives in Biology","month":"02","oa_version":"None","keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"external_id":{"pmid":["20300205"]},"year":"2010","citation":{"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>.","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>","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>","ista":"Hetzer M. 2010. The nuclear envelope. Cold Spring Harbor Perspectives in Biology. 2(3), a000539–a000539.","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>."},"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"}],"day":"03","doi":"10.1101/cshperspect.a000539","extern":"1","volume":2,"issue":"3","author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"scopus_import":"1","pmid":1,"_id":"11097","intvolume":"         2","title":"The nuclear envelope","date_created":"2022-04-07T07:52:49Z","article_processing_charge":"No","publication_status":"published","quality_controlled":"1","page":"a000539-a000539","article_type":"original","publisher":"Cold Spring Harbor Laboratory"},{"intvolume":"       141","title":"Cell cycle-dependent differences in nuclear pore complex assembly in metazoa","date_created":"2022-04-07T07:53:29Z","article_processing_charge":"No","publication_status":"published","issue":"6","author":[{"full_name":"Doucet, Christine M.","last_name":"Doucet","first_name":"Christine M."},{"full_name":"Talamas, Jessica A.","first_name":"Jessica A.","last_name":"Talamas"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"scopus_import":"1","_id":"11101","pmid":1,"article_type":"original","publisher":"Elsevier","quality_controlled":"1","page":"1030-1041","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"}],"day":"11","doi":"10.1016/j.cell.2010.04.036","external_id":{"pmid":["20550937"]},"citation":{"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>","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>","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.","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.","ista":"Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041."},"year":"2010","date_updated":"2022-07-18T08:54:52Z","extern":"1","volume":141,"month":"06","oa_version":"Published Version","publication":"Cell","keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"oa":1,"publication_identifier":{"issn":["0092-8674"]},"type":"journal_article","date_published":"2010-06-11T00:00:00Z","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2010.04.036"}]},{"extern":"1","volume":140,"external_id":{"pmid":["20144761"]},"date_updated":"2022-07-18T08:55:03Z","year":"2010","citation":{"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.","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>","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>","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."},"abstract":[{"lang":"eng","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."}],"doi":"10.1016/j.cell.2009.12.054","day":"05","page":"372-383","quality_controlled":"1","article_type":"original","publisher":"Elsevier","author":[{"full_name":"Capelson, Maya","last_name":"Capelson","first_name":"Maya"},{"full_name":"Liang, Yun","first_name":"Yun","last_name":"Liang"},{"full_name":"Schulte, Roberta","first_name":"Roberta","last_name":"Schulte"},{"full_name":"Mair, William","last_name":"Mair","first_name":"William"},{"first_name":"Ulrich","last_name":"Wagner","full_name":"Wagner, Ulrich"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"issue":"3","_id":"11102","pmid":1,"scopus_import":"1","title":"Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes","intvolume":"       140","publication_status":"published","date_created":"2022-04-07T07:53:36Z","article_processing_charge":"No","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2009.12.054"}],"date_published":"2010-02-05T00:00:00Z","type":"journal_article","oa":1,"publication_identifier":{"issn":["0092-8674"]},"language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"publication":"Cell","month":"02","oa_version":"Published Version"},{"type":"journal_article","date_published":"2010-02-19T00:00:00Z","citation":{"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.","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.","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.","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>."},"year":"2010","date_updated":"2021-01-12T08:19:31Z","abstract":[{"lang":"eng","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."}],"day":"19","publication_identifier":{"issn":["0021-9258","1083-351X"]},"doi":"10.1074/jbc.m109.061168","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","volume":285,"issue":"8","author":[{"last_name":"Corazza","first_name":"Alessandra","full_name":"Corazza, Alessandra"},{"full_name":"Rennella, Enrico","first_name":"Enrico","last_name":"Rennella"},{"first_name":"Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"last_name":"Mimmi","first_name":"Maria Chiara","full_name":"Mimmi, Maria Chiara"},{"last_name":"Cutuil","first_name":"Thomas","full_name":"Cutuil, Thomas"},{"first_name":"Sara","last_name":"Raimondi","full_name":"Raimondi, Sara"},{"full_name":"Giorgetti, Sofia","first_name":"Sofia","last_name":"Giorgetti"},{"first_name":"Federico","last_name":"Fogolari","full_name":"Fogolari, Federico"},{"last_name":"Viglino","first_name":"Paolo","full_name":"Viglino, Paolo"},{"full_name":"Frydman, Lucio","last_name":"Frydman","first_name":"Lucio"},{"full_name":"Gal, Maayan","last_name":"Gal","first_name":"Maayan"},{"full_name":"Bellotti, Vittorio","last_name":"Bellotti","first_name":"Vittorio"},{"full_name":"Brutscher, Bernhard","first_name":"Bernhard","last_name":"Brutscher"},{"last_name":"Esposito","first_name":"Gennaro","full_name":"Esposito, Gennaro"}],"publication":"Journal of Biological Chemistry","_id":"8473","intvolume":"       285","title":"Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR","month":"02","article_processing_charge":"No","date_created":"2020-09-18T10:11:23Z","oa_version":"None","publication_status":"published","keyword":["Cell Biology","Biochemistry","Molecular Biology"],"language":[{"iso":"eng"}],"quality_controlled":"1","page":"5827-5835","article_type":"original","publisher":"American Society for Biochemistry & Molecular Biology"},{"volume":132,"extern":"1","year":"2010","citation":{"apa":"Coskun, A., Wesson, P. J., Klajn, R., Trabolsi, A., Fang, L., Olson, M. A., … Stoddart, J. F. (2010). Molecular-mechanical switching at the nanoparticle−solvent interface: Practice and theory. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja9102327\">https://doi.org/10.1021/ja9102327</a>","ama":"Coskun A, Wesson PJ, Klajn R, et al. Molecular-mechanical switching at the nanoparticle−solvent interface: Practice and theory. <i>Journal of the American Chemical Society</i>. 2010;132(12):4310-4320. doi:<a href=\"https://doi.org/10.1021/ja9102327\">10.1021/ja9102327</a>","chicago":"Coskun, Ali, Paul J. Wesson, Rafal Klajn, Ali Trabolsi, Lei Fang, Mark A. Olson, Sanjeev K. Dey, Bartosz A. Grzybowski, and J. Fraser Stoddart. “Molecular-Mechanical Switching at the Nanoparticle−solvent Interface: Practice and Theory.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2010. <a href=\"https://doi.org/10.1021/ja9102327\">https://doi.org/10.1021/ja9102327</a>.","ieee":"A. Coskun <i>et al.</i>, “Molecular-mechanical switching at the nanoparticle−solvent interface: Practice and theory,” <i>Journal of the American Chemical Society</i>, vol. 132, no. 12. American Chemical Society, pp. 4310–4320, 2010.","mla":"Coskun, Ali, et al. “Molecular-Mechanical Switching at the Nanoparticle−solvent Interface: Practice and Theory.” <i>Journal of the American Chemical Society</i>, vol. 132, no. 12, American Chemical Society, 2010, pp. 4310–20, doi:<a href=\"https://doi.org/10.1021/ja9102327\">10.1021/ja9102327</a>.","short":"A. Coskun, P.J. Wesson, R. Klajn, A. Trabolsi, L. Fang, M.A. Olson, S.K. Dey, B.A. Grzybowski, J.F. Stoddart, Journal of the American Chemical Society 132 (2010) 4310–4320.","ista":"Coskun A, Wesson PJ, Klajn R, Trabolsi A, Fang L, Olson MA, Dey SK, Grzybowski BA, Stoddart JF. 2010. Molecular-mechanical switching at the nanoparticle−solvent interface: Practice and theory. Journal of the American Chemical Society. 132(12), 4310–4320."},"date_updated":"2023-08-08T08:00:31Z","external_id":{"pmid":["20218598"]},"day":"31","doi":"10.1021/ja9102327","abstract":[{"lang":"eng","text":"A range (Au, Pt, Pd) of metal nanoparticles (MNPs) has been prepared and functionalized with (a) redox-active stalks containing tetrathiafulvalene (TTF) units, (b) [2]pseudorotaxanes formed between these stalks and cyclobis(paraquat-p-phenylene) (CBPQT4+) rings, and (c) bistable [2]rotaxane molecules where the dumbbell component contains a 1,5-dioxynaphthalene (DNP) unit, as well as a TTF unit, encircled by a CBPQT4+ ring. It transpires that the molecules present in (a) and (c) and the supermolecules described in (b) retain their switching characteristics, previously observed in solution, when they are immobilized onto MNPs. Moreover, their oxidation potentials depend on the fraction, χ, of the molecules or supermolecules on the surface of the nanoparticles. A variation in χ affects the oxidation potentials of the TTF units to the extent that switching can be subjected to fine tuning as a result. Specifically, increasing χ results in positive shifts (i) in the oxidation potentials of the TTF unit in (a)−(c) and (ii) the reduction potentials of the CBPQT4+ rings in (c). These shifts can be attributed to an increase in the electrostatic potential surrounding the MNPs. Both the magnitude and the direction of these shifts are reproduced by a model, based on the Poisson−Boltzmann equation coupled with charge-regulating boundary conditions. Furthermore, the kinetics of relaxation from the metastable state coconformation (MSCC) to the ground-state coconformation (GSCC) of the bistable [2]rotaxane molecules also depends on χ, as well as on the nanoparticle diameter. Increasing either of these parameters accelerates the rate of relaxation from the MSCC to the GSCC. This rate is a function of (i) the activation energy for the relaxation process associated with the bistable [2]rotaxane molecules in solution and (ii) the electrostatic potential surrounding the MNPs. The electrostatic potential depends on (i) the diameter of the MNPs, (ii) the amount of the bistable [2]rotaxane molecules on the surface of the MNPs, and (iii) the equilibrium distribution of the CBPQT4+ rings between the DNP and TTF recognition sites in the GSCC. This electrostatic potential has also been quantified using the Poisson−Boltzmann equation, leading to faithful estimates of the rate constants."}],"quality_controlled":"1","page":"4310-4320","publisher":"American Chemical Society","article_type":"original","scopus_import":"1","_id":"13410","pmid":1,"issue":"12","author":[{"full_name":"Coskun, Ali","last_name":"Coskun","first_name":"Ali"},{"first_name":"Paul J.","last_name":"Wesson","full_name":"Wesson, Paul J."},{"id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn","first_name":"Rafal","full_name":"Klajn, Rafal"},{"first_name":"Ali","last_name":"Trabolsi","full_name":"Trabolsi, Ali"},{"full_name":"Fang, Lei","first_name":"Lei","last_name":"Fang"},{"first_name":"Mark A.","last_name":"Olson","full_name":"Olson, Mark A."},{"full_name":"Dey, Sanjeev K.","last_name":"Dey","first_name":"Sanjeev K."},{"last_name":"Grzybowski","first_name":"Bartosz A.","full_name":"Grzybowski, Bartosz A."},{"full_name":"Stoddart, J. Fraser","first_name":"J. Fraser","last_name":"Stoddart"}],"date_created":"2023-08-01T09:48:27Z","article_processing_charge":"No","publication_status":"published","intvolume":"       132","title":"Molecular-mechanical switching at the nanoparticle−solvent interface: Practice and theory","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","type":"journal_article","date_published":"2010-03-31T00:00:00Z","publication_identifier":{"eissn":["1520-5126"],"issn":["0002-7863"]},"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"language":[{"iso":"eng"}],"publication":"Journal of the American Chemical Society","oa_version":"None","month":"03"},{"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","type":"journal_article","date_published":"2010-03-22T00:00:00Z","publication_identifier":{"issn":["0300-5127","1470-8752"]},"keyword":["Biochemistry","Anther Development","Arabidopsis","Cell Fate","Microsporangium","Polarity","Receptor Kinase"],"language":[{"iso":"eng"}],"publication":"Biochemical Society Transactions","oa_version":"None","month":"03","volume":38,"extern":"1","year":"2010","citation":{"chicago":"Feng, Xiaoqi, and Hugh G. Dickinson. “Cell–Cell Interactions during Patterning of the <i>Arabidopsis</i> Anther.” <i>Biochemical Society Transactions</i>. Portland Press Ltd., 2010. <a href=\"https://doi.org/10.1042/bst0380571\">https://doi.org/10.1042/bst0380571</a>.","ieee":"X. Feng and H. G. Dickinson, “Cell–cell interactions during patterning of the <i>Arabidopsis</i> anther,” <i>Biochemical Society Transactions</i>, vol. 38, no. 2. Portland Press Ltd., pp. 571–576, 2010.","apa":"Feng, X., &#38; Dickinson, H. G. (2010). Cell–cell interactions during patterning of the <i>Arabidopsis</i> anther. <i>Biochemical Society Transactions</i>. Portland Press Ltd. <a href=\"https://doi.org/10.1042/bst0380571\">https://doi.org/10.1042/bst0380571</a>","ama":"Feng X, Dickinson HG. Cell–cell interactions during patterning of the <i>Arabidopsis</i> anther. <i>Biochemical Society Transactions</i>. 2010;38(2):571-576. doi:<a href=\"https://doi.org/10.1042/bst0380571\">10.1042/bst0380571</a>","ista":"Feng X, Dickinson HG. 2010. Cell–cell interactions during patterning of the <i>Arabidopsis</i> anther. Biochemical Society Transactions. 38(2), 571–576.","short":"X. Feng, H.G. Dickinson, Biochemical Society Transactions 38 (2010) 571–576.","mla":"Feng, Xiaoqi, and Hugh G. Dickinson. “Cell–Cell Interactions during Patterning of the <i>Arabidopsis</i> Anther.” <i>Biochemical Society Transactions</i>, vol. 38, no. 2, Portland Press Ltd., 2010, pp. 571–76, doi:<a href=\"https://doi.org/10.1042/bst0380571\">10.1042/bst0380571</a>."},"date_updated":"2023-05-08T10:57:59Z","external_id":{"pmid":["20298223"]},"day":"22","doi":"10.1042/bst0380571","abstract":[{"lang":"eng","text":"Key steps in the evolution of the angiosperm anther include the patterning of the concentrically organized microsporangium and the incorporation of four such microsporangia into a leaf-like structure. Mutant studies in the model plant Arabidopsis thaliana are leading to an increasingly accurate picture of (i) the cell lineages culminating in the different cell types present in the microsporangium (the microsporocytes, the tapetum, and the middle and endothecial layers), and (ii) some of the genes responsible for specifying their fates. However, the processes that confer polarity on the developing anther and position the microsporangia within it remain unclear. Certainly, data from a range of experimental strategies suggest that hormones play a central role in establishing polarity and the patterning of the anther initial, and may be responsible for locating the microsporangia. But the fact that microsporangia were originally positioned externally suggests that their development is likely to be autonomous, perhaps with the reproductive cells generating signals controlling the growth and division of the investing anther epidermis. These possibilities are discussed in the context of the expression of genes which initiate and maintain male and female reproductive development, and in the perspective of our current views of anther evolution."}],"quality_controlled":"1","page":"571-576","publisher":"Portland Press Ltd.","article_type":"original","scopus_import":"1","_id":"12200","pmid":1,"issue":"2","author":[{"id":"e0164712-22ee-11ed-b12a-d80fcdf35958","full_name":"Feng, Xiaoqi","orcid":"0000-0002-4008-1234","last_name":"Feng","first_name":"Xiaoqi"},{"last_name":"Dickinson","first_name":"Hugh G.","full_name":"Dickinson, Hugh G."}],"department":[{"_id":"XiFe"}],"date_created":"2023-01-16T09:22:18Z","article_processing_charge":"No","publication_status":"published","intvolume":"        38","title":"Cell–cell interactions during patterning of the <i>Arabidopsis</i> anther"},{"external_id":{"pmid":["19922866"]},"date_updated":"2022-07-18T08:55:01Z","citation":{"ama":"Hetzer M, Wente SR. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. <i>Developmental Cell</i>. 2009;17(5):606-616. doi:<a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">10.1016/j.devcel.2009.10.007</a>","apa":"Hetzer, M., &#38; Wente, S. R. (2009). Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. <i>Developmental Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">https://doi.org/10.1016/j.devcel.2009.10.007</a>","chicago":"Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis and Organization of the Nuclear Membrane and Pore Complexes.” <i>Developmental Cell</i>. Elsevier, 2009. <a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">https://doi.org/10.1016/j.devcel.2009.10.007</a>.","ieee":"M. Hetzer and S. R. Wente, “Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes,” <i>Developmental Cell</i>, vol. 17, no. 5. Elsevier, pp. 606–616, 2009.","short":"M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.","mla":"Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis and Organization of the Nuclear Membrane and Pore Complexes.” <i>Developmental Cell</i>, vol. 17, no. 5, Elsevier, 2009, pp. 606–16, doi:<a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">10.1016/j.devcel.2009.10.007</a>.","ista":"Hetzer M, Wente SR. 2009. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. Developmental Cell. 17(5), 606–616."},"year":"2009","abstract":[{"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.","lang":"eng"}],"doi":"10.1016/j.devcel.2009.10.007","day":"17","extern":"1","volume":17,"author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"},{"full_name":"Wente, Susan R.","last_name":"Wente","first_name":"Susan R."}],"issue":"5","pmid":1,"_id":"11103","scopus_import":"1","title":"Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes","intvolume":"        17","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:53:45Z","page":"606-616","quality_controlled":"1","article_type":"review","publisher":"Elsevier","date_published":"2009-11-17T00:00:00Z","type":"journal_article","oa":1,"publication_identifier":{"issn":["1534-5807"]},"status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"url":"https://doi.org/10.1016/j.devcel.2009.10.007","open_access":"1"}],"publication":"Developmental Cell","month":"11","oa_version":"Published Version","language":[{"iso":"eng"}],"keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"]},{"keyword":["Genetics","Molecular Biology","Biochemistry"],"language":[{"iso":"eng"}],"publication":"EMBO reports","month":"07","oa_version":"Published Version","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/embor.2009.176"}]},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/embor.2009.147"}],"type":"journal_article","date_published":"2009-07-01T00:00:00Z","oa":1,"publication_identifier":{"eissn":["1469-3178"],"issn":["1469-221X"]},"quality_controlled":"1","page":"697-705","article_type":"original","publisher":"EMBO","issue":"7","author":[{"full_name":"Capelson, Maya","last_name":"Capelson","first_name":"Maya"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"scopus_import":"1","pmid":1,"_id":"11105","intvolume":"        10","title":"The role of nuclear pores in gene regulation, development and disease","date_created":"2022-04-07T07:54:06Z","article_processing_charge":"No","publication_status":"published","extern":"1","volume":10,"external_id":{"pmid":["19543230"]},"citation":{"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.","ista":"Capelson M, Hetzer M. 2009. The role of nuclear pores in gene regulation, development and disease. EMBO reports. 10(7), 697–705.","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>","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>","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>.","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."},"year":"2009","date_updated":"2022-07-18T08:42:44Z","abstract":[{"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.","lang":"eng"}],"day":"01","doi":"10.1038/embor.2009.147"},{"date_updated":"2022-07-18T08:55:29Z","citation":{"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.","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.","ieee":"M. A. D’Angelo, M. Raices, S. H. Panowski, and M. Hetzer, “Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells,” <i>Cell</i>, vol. 136, no. 2. Elsevier, pp. 284–295, 2009.","chicago":"D’Angelo, Maximiliano A., Marcela Raices, Siler H. Panowski, and Martin Hetzer. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” <i>Cell</i>. Elsevier, 2009. <a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">https://doi.org/10.1016/j.cell.2008.11.037</a>.","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>","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>"},"year":"2009","external_id":{"pmid":["19167330"]},"doi":"10.1016/j.cell.2008.11.037","day":"23","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"}],"volume":136,"extern":"1","_id":"11108","pmid":1,"scopus_import":"1","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"},{"full_name":"Panowski, Siler H.","first_name":"Siler H.","last_name":"Panowski"},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"issue":"2","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:54:52Z","title":"Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells","intvolume":"       136","page":"284-295","quality_controlled":"1","publisher":"Elsevier","article_type":"original","date_published":"2009-01-23T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["0092-8674"]},"oa":1,"main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2008.11.037","open_access":"1"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","publication":"Cell","oa_version":"Published Version","month":"01","language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"]},{"author":[{"first_name":"Maayan","last_name":"Gal","full_name":"Gal, Maayan"},{"first_name":"Thomas","last_name":"Kern","full_name":"Kern, Thomas"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606"},{"first_name":"Lucio","last_name":"Frydman","full_name":"Frydman, Lucio"},{"full_name":"Brutscher, Bernhard","first_name":"Bernhard","last_name":"Brutscher"}],"_id":"8479","publication":"Journal of Biomolecular NMR","month":"01","title":"An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates","intvolume":"        43","oa_version":"None","publication_status":"published","date_created":"2020-09-18T10:12:20Z","article_processing_charge":"No","language":[{"iso":"eng"}],"keyword":["Spectroscopy","Biochemistry"],"page":"1-10","quality_controlled":"1","article_type":"original","publisher":"Springer Nature","date_published":"2009-01-01T00:00:00Z","type":"journal_article","date_updated":"2021-01-12T08:19:33Z","citation":{"ista":"Gal M, Kern T, Schanda P, Frydman L, Brutscher B. 2009. An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. Journal of Biomolecular NMR. 43, 1–10.","mla":"Gal, Maayan, et al. “An Improved Ultrafast 2D NMR Experiment: Towards Atom-Resolved Real-Time Studies of Protein Kinetics at Multi-Hz Rates.” <i>Journal of Biomolecular NMR</i>, vol. 43, Springer Nature, 2009, pp. 1–10, doi:<a href=\"https://doi.org/10.1007/s10858-008-9284-9\">10.1007/s10858-008-9284-9</a>.","short":"M. Gal, T. Kern, P. Schanda, L. Frydman, B. Brutscher, Journal of Biomolecular NMR 43 (2009) 1–10.","chicago":"Gal, Maayan, Thomas Kern, Paul Schanda, Lucio Frydman, and Bernhard Brutscher. “An Improved Ultrafast 2D NMR Experiment: Towards Atom-Resolved Real-Time Studies of Protein Kinetics at Multi-Hz Rates.” <i>Journal of Biomolecular NMR</i>. Springer Nature, 2009. <a href=\"https://doi.org/10.1007/s10858-008-9284-9\">https://doi.org/10.1007/s10858-008-9284-9</a>.","ieee":"M. Gal, T. Kern, P. Schanda, L. Frydman, and B. Brutscher, “An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates,” <i>Journal of Biomolecular NMR</i>, vol. 43. Springer Nature, pp. 1–10, 2009.","ama":"Gal M, Kern T, Schanda P, Frydman L, Brutscher B. An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. <i>Journal of Biomolecular NMR</i>. 2009;43:1-10. doi:<a href=\"https://doi.org/10.1007/s10858-008-9284-9\">10.1007/s10858-008-9284-9</a>","apa":"Gal, M., Kern, T., Schanda, P., Frydman, L., &#38; Brutscher, B. (2009). An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. <i>Journal of Biomolecular NMR</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s10858-008-9284-9\">https://doi.org/10.1007/s10858-008-9284-9</a>"},"year":"2009","abstract":[{"lang":"eng","text":"Multidimensional NMR spectroscopy is a well-established technique for the characterization of structure and fast-time-scale dynamics of highly populated ground states of biological macromolecules. The investigation of short-lived excited states that are important for molecular folding, misfolding and function, however, remains a challenge for modern biomolecular NMR techniques. Off-equilibrium real-time kinetic NMR methods allow direct observation of conformational or chemical changes by following peak positions and intensities in a series of spectra recorded during a kinetic event. Because standard multidimensional NMR methods required to yield sufficient atom-resolution are intrinsically time-consuming, many interesting phenomena are excluded from real-time NMR analysis. Recently, spatially encoded ultrafast 2D NMR techniques have been proposed that allow one to acquire a 2D NMR experiment within a single transient. In addition, when combined with the SOFAST technique, such ultrafast experiments can be repeated at high rates. One of the problems detected for such ultrafast protein NMR experiments is related to the heteronuclear decoupling during detection with interferences between the pulses and the oscillatory magnetic field gradients arising in this scheme. Here we present a method for improved ultrafast data acquisition yielding higher signal to noise and sharper lines in single-scan 2D NMR spectra. In combination with a fast-mixing device, the recording of 1H–15N correlation spectra with repetition rates of up to a few Hertz becomes feasible, enabling real-time studies of protein kinetics occurring on time scales down to a few seconds."}],"doi":"10.1007/s10858-008-9284-9","publication_identifier":{"issn":["0925-2738","1573-5001"]},"day":"01","extern":"1","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","volume":43},{"publication_status":"published","date_created":"2023-08-01T10:30:17Z","article_processing_charge":"No","title":"Metal nanoparticles functionalized with molecular and supramolecular switches","intvolume":"       131","_id":"13420","pmid":1,"scopus_import":"1","author":[{"full_name":"Klajn, Rafal","first_name":"Rafal","last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"},{"full_name":"Fang, Lei","first_name":"Lei","last_name":"Fang"},{"last_name":"Coskun","first_name":"Ali","full_name":"Coskun, Ali"},{"full_name":"Olson, Mark A.","last_name":"Olson","first_name":"Mark A."},{"last_name":"Wesson","first_name":"Paul J.","full_name":"Wesson, Paul J."},{"full_name":"Stoddart, J. Fraser","first_name":"J. Fraser","last_name":"Stoddart"},{"full_name":"Grzybowski, Bartosz A.","first_name":"Bartosz A.","last_name":"Grzybowski"}],"issue":"12","publisher":"American Chemical Society","article_type":"original","page":"4233-4235","quality_controlled":"1","doi":"10.1021/ja9001585","day":"01","abstract":[{"text":"Weakly protected metal nanoparticles (MNPs) are used as precursors for the preparation of catenane- and pseudorotaxane-decorated NPs of various compositions (gold, palladium, platinum). When attached to the surface of MNPs, the molecular switches retain their switching abilities. The redox potentials of these switches depend on and can be regulated by the composition of the mixed self-assembled monolayers covering the MNPs.","lang":"eng"}],"date_updated":"2023-08-08T09:06:00Z","citation":{"ista":"Klajn R, Fang L, Coskun A, Olson MA, Wesson PJ, Stoddart JF, Grzybowski BA. 2009. Metal nanoparticles functionalized with molecular and supramolecular switches. Journal of the American Chemical Society. 131(12), 4233–4235.","short":"R. Klajn, L. Fang, A. Coskun, M.A. Olson, P.J. Wesson, J.F. Stoddart, B.A. Grzybowski, Journal of the American Chemical Society 131 (2009) 4233–4235.","mla":"Klajn, Rafal, et al. “Metal Nanoparticles Functionalized with Molecular and Supramolecular Switches.” <i>Journal of the American Chemical Society</i>, vol. 131, no. 12, American Chemical Society, 2009, pp. 4233–35, doi:<a href=\"https://doi.org/10.1021/ja9001585\">10.1021/ja9001585</a>.","chicago":"Klajn, Rafal, Lei Fang, Ali Coskun, Mark A. Olson, Paul J. Wesson, J. Fraser Stoddart, and Bartosz A. Grzybowski. “Metal Nanoparticles Functionalized with Molecular and Supramolecular Switches.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2009. <a href=\"https://doi.org/10.1021/ja9001585\">https://doi.org/10.1021/ja9001585</a>.","ieee":"R. Klajn <i>et al.</i>, “Metal nanoparticles functionalized with molecular and supramolecular switches,” <i>Journal of the American Chemical Society</i>, vol. 131, no. 12. American Chemical Society, pp. 4233–4235, 2009.","ama":"Klajn R, Fang L, Coskun A, et al. Metal nanoparticles functionalized with molecular and supramolecular switches. <i>Journal of the American Chemical Society</i>. 2009;131(12):4233-4235. doi:<a href=\"https://doi.org/10.1021/ja9001585\">10.1021/ja9001585</a>","apa":"Klajn, R., Fang, L., Coskun, A., Olson, M. A., Wesson, P. J., Stoddart, J. F., &#38; Grzybowski, B. A. (2009). Metal nanoparticles functionalized with molecular and supramolecular switches. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja9001585\">https://doi.org/10.1021/ja9001585</a>"},"year":"2009","external_id":{"pmid":["19265400"]},"volume":131,"extern":"1","oa_version":"None","month":"04","publication":"Journal of the American Chemical Society","language":[{"iso":"eng"}],"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"date_published":"2009-04-01T00:00:00Z","type":"journal_article","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87"}]