[{"day":"07","publication_status":"published","type":"journal_article","volume":5,"external_id":{"pmid":["24709950"]},"publisher":"Springer Nature","language":[{"iso":"eng"}],"year":"2014","_id":"13402","title":"Nanoporous frameworks exhibiting multiple stimuli responsiveness","publication":"Nature Communications","doi":"10.1038/ncomms4588","date_updated":"2024-10-14T12:20:30Z","intvolume":"         5","pmid":1,"citation":{"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.","ieee":"P. K. Kundu, G. L. Olsen, V. Kiss, and R. Klajn, “Nanoporous frameworks exhibiting multiple stimuli responsiveness,” <i>Nature Communications</i>, vol. 5. Springer Nature, 2014.","chicago":"Kundu, Pintu K., Gregory L. Olsen, Vladimir Kiss, and Rafal Klajn. “Nanoporous Frameworks Exhibiting Multiple Stimuli Responsiveness.” <i>Nature Communications</i>. Springer Nature, 2014. <a href=\"https://doi.org/10.1038/ncomms4588\">https://doi.org/10.1038/ncomms4588</a>.","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>","short":"P.K. Kundu, G.L. Olsen, V. Kiss, R. Klajn, Nature Communications 5 (2014)."},"abstract":[{"text":"Nanoporous frameworks are polymeric materials built from rigid molecules, which give rise to their nanoporous structures with applications in gas sorption and storage, catalysis and others. Conceptually new applications could emerge, should these beneficial properties be manipulated by external stimuli in a reversible manner. One approach to render nanoporous frameworks responsive to external signals would be to immobilize molecular switches within their nanopores. Although the majority of molecular switches require conformational freedom to isomerize, and switching in the solid state is prohibited, the nanopores may provide enough room for the switches to efficiently isomerize. Here we describe two families of nanoporous materials incorporating the spiropyran molecular switch. These materials exhibit a variety of interesting properties, including reversible photochromism and acidochromism under solvent-free conditions, light-controlled capture and release of metal ions, as well reversible chromism induced by solvation/desolvation.","lang":"eng"}],"publication_identifier":{"eissn":["2041-1723"]},"article_number":"3588","oa_version":"Published Version","quality_controlled":"1","article_type":"original","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"article_processing_charge":"No","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms4588"}],"month":"04","status":"public","fulldoi":"https://doi.org/10.1038/ncomms4588","date_published":"2014-04-07T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":"1","author":[{"first_name":"Pintu K.","last_name":"Kundu","full_name":"Kundu, Pintu K."},{"last_name":"Olsen","full_name":"Olsen, Gregory L.","first_name":"Gregory L."},{"last_name":"Kiss","full_name":"Kiss, Vladimir","first_name":"Vladimir"},{"last_name":"Klajn","full_name":"Klajn, Rafal","first_name":"Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"oa":1,"date_created":"2023-08-01T09:46:27Z","extern":"1"},{"status":"public","fulldoi":"https://doi.org/10.1016/j.cell.2013.06.007","date_published":"2013-07-03T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"first_name":"Emily M.","last_name":"Hatch","full_name":"Hatch, Emily M."},{"first_name":"Andrew H.","full_name":"Fischer, Andrew H.","last_name":"Fischer"},{"full_name":"Deerinck, Thomas J.","last_name":"Deerinck","first_name":"Thomas J."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","first_name":"Martin W","last_name":"HETZER","full_name":"HETZER, Martin W"}],"scopus_import":"1","oa":1,"extern":"1","date_created":"2022-04-07T07:50:51Z","quality_controlled":"1","oa_version":"Published Version","article_type":"original","article_processing_charge":"No","keyword":["General Biochemistry","Genetics and Molecular Biology"],"main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2013.06.007","open_access":"1"}],"month":"07","doi":"10.1016/j.cell.2013.06.007","date_updated":"2024-10-14T11:24:29Z","issue":"1","pmid":1,"citation":{"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>.","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>","short":"E.M. Hatch, A.H. Fischer, T.J. Deerinck, M. Hetzer, Cell 154 (2013) 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>","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>.","ista":"Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. 2013. Catastrophic nuclear envelope collapse in cancer cell micronuclei. Cell. 154(1), 47–60.","ieee":"E. M. Hatch, A. H. Fischer, T. J. Deerinck, and M. Hetzer, “Catastrophic nuclear envelope collapse in cancer cell micronuclei,” <i>Cell</i>, vol. 154, no. 1. Elsevier, pp. 47–60, 2013."},"intvolume":"       154","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"}],"publication_identifier":{"issn":["0092-8674"]},"day":"03","publication_status":"published","type":"journal_article","external_id":{"pmid":["23827674"]},"volume":154,"publisher":"Elsevier","year":"2013","_id":"11085","page":"47-60","language":[{"iso":"eng"}],"publication":"Cell","title":"Catastrophic nuclear envelope collapse in cancer cell micronuclei"},{"department":[{"_id":"MaHe"}],"oa_version":"Published Version","OA_place":"publisher","quality_controlled":"1","OA_type":"free access","article_type":"original","keyword":["General Biochemistry","Genetics and Molecular Biology"],"article_processing_charge":"No","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2013.07.037"}],"month":"08","fulldoi":"https://doi.org/10.1016/j.cell.2013.07.037","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2013-08-29T00:00:00Z","scopus_import":"1","author":[{"last_name":"Toyama","full_name":"Toyama, Brandon H.","first_name":"Brandon H."},{"first_name":"Jeffrey N.","last_name":"Savas","full_name":"Savas, Jeffrey N."},{"first_name":"Sung Kyu","full_name":"Park, Sung Kyu","last_name":"Park"},{"first_name":"Michael S.","full_name":"Harris, Michael S.","last_name":"Harris"},{"full_name":"Ingolia, Nicholas T.","last_name":"Ingolia","first_name":"Nicholas T."},{"last_name":"Yates","full_name":"Yates, John R.","first_name":"John R."},{"full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"oa":1,"date_created":"2022-04-07T07:51:08Z","extern":"1","day":"29","publication_status":"published","type":"journal_article","volume":154,"external_id":{"pmid":["23993091"]},"publisher":"Elsevier","page":"971-982","language":[{"iso":"eng"}],"_id":"11087","year":"2013","title":"Identification of long-lived proteins reveals exceptional stability of essential cellular structures","publication":"Cell","doi":"10.1016/j.cell.2013.07.037","issue":"5","date_updated":"2026-07-28T10:15:26Z","intvolume":"       154","pmid":1,"citation":{"ieee":"B. H. Toyama <i>et al.</i>, “Identification of long-lived proteins reveals exceptional stability of essential cellular structures,” <i>Cell</i>, vol. 154, no. 5. Elsevier, pp. 971–982, 2013.","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>.","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>","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.","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>."},"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"}],"publication_identifier":{"issn":["0092-8674"]},"das_tickbox":"1"},{"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."}],"publication_identifier":{"issn":["0092-8674"]},"doi":"10.1016/j.cell.2012.04.018","date_updated":"2024-10-14T11:25:24Z","issue":"4","intvolume":"       149","pmid":1,"citation":{"apa":"Hatch, E. M., &#38; Hetzer, M. (2012). RNP export by nuclear envelope budding. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">https://doi.org/10.1016/j.cell.2012.04.018</a>","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>.","ista":"Hatch EM, Hetzer M. 2012. RNP export by nuclear envelope budding. Cell. 149(4), 733–735.","ieee":"E. M. Hatch and M. Hetzer, “RNP export by nuclear envelope budding,” <i>Cell</i>, vol. 149, no. 4. Elsevier, pp. 733–735, 2012.","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>.","short":"E.M. Hatch, M. Hetzer, Cell 149 (2012) 733–735.","ama":"Hatch EM, Hetzer M. RNP export by nuclear envelope budding. <i>Cell</i>. 2012;149(4):733-735. doi:<a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">10.1016/j.cell.2012.04.018</a>"},"volume":149,"external_id":{"pmid":["22579277"]},"publisher":"Elsevier","language":[{"iso":"eng"}],"page":"733-735","year":"2012","_id":"11090","title":"RNP export by nuclear envelope budding","publication":"Cell","day":"11","publication_status":"published","type":"journal_article","oa":1,"date_created":"2022-04-07T07:51:45Z","extern":"1","fulldoi":"https://doi.org/10.1016/j.cell.2012.04.018","status":"public","date_published":"2012-05-11T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":"1","author":[{"last_name":"Hatch","full_name":"Hatch, Emily M.","first_name":"Emily M."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER"}],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2012.04.018"}],"month":"05","oa_version":"Published Version","quality_controlled":"1","article_type":"letter_note","article_processing_charge":"No","keyword":["General Biochemistry","Genetics and Molecular Biology"]},{"publication_status":"published","day":"19","type":"journal_article","publisher":"Elsevier","external_id":{"pmid":["22264802"]},"volume":22,"publication":"Developmental Cell","title":"A change in nuclear pore complex composition regulates cell differentiation","year":"2012","_id":"11093","page":"446-458","language":[{"iso":"eng"}],"date_updated":"2024-10-14T11:26:00Z","issue":"2","doi":"10.1016/j.devcel.2011.11.021","citation":{"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>.","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.","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>","short":"M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental Cell 22 (2012) 446–458."},"pmid":1,"intvolume":"        22","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"}],"publication_identifier":{"issn":["1534-5807"]},"article_type":"original","quality_controlled":"1","oa_version":"Published Version","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"article_processing_charge":"No","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2011.11.021"}],"month":"01","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2012-01-19T00:00:00Z","fulldoi":"https://doi.org/10.1016/j.devcel.2011.11.021","status":"public","author":[{"first_name":"Maximiliano A.","last_name":"D'Angelo","full_name":"D'Angelo, Maximiliano A."},{"first_name":"J. Sebastian","last_name":"Gomez-Cavazos","full_name":"Gomez-Cavazos, J. Sebastian"},{"first_name":"Arianna","last_name":"Mei","full_name":"Mei, Arianna"},{"first_name":"Daniel H.","last_name":"Lackner","full_name":"Lackner, Daniel H."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER"}],"scopus_import":"1","extern":"1","date_created":"2022-04-07T07:52:10Z","oa":1},{"abstract":[{"lang":"eng","text":"The nuclear envelope (NE) is a highly regulated membrane barrier that separates the nucleus from the cytoplasm in eukaryotic cells. It contains a large number of different proteins that have been implicated in chromatin organization and gene regulation. Although the nuclear membrane enables complex levels of gene expression, it also poses a challenge when it comes to cell division. To allow access of the mitotic spindle to chromatin, the nucleus of metazoans must completely disassemble during mitosis, generating the need to re-establish the nuclear compartment at the end of each cell division. Here, I summarize our current understanding of the dynamic remodeling of the NE during the cell cycle."}],"publication_identifier":{"issn":["1943-0264"]},"issue":"3","date_updated":"2024-10-14T11:26:41Z","doi":"10.1101/cshperspect.a000539","pmid":1,"citation":{"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>","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>","short":"M. Hetzer, Cold Spring Harbor Perspectives in Biology 2 (2010) a000539–a000539.","ista":"Hetzer M. 2010. The nuclear envelope. Cold Spring Harbor Perspectives in Biology. 2(3), a000539–a000539.","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>."},"intvolume":"         2","publisher":"Cold Spring Harbor Laboratory","external_id":{"pmid":["20300205"]},"volume":2,"publication":"Cold Spring Harbor Perspectives in Biology","title":"The nuclear envelope","year":"2010","_id":"11097","page":"a000539-a000539","language":[{"iso":"eng"}],"publication_status":"published","day":"03","type":"journal_article","extern":"1","date_created":"2022-04-07T07:52:49Z","date_published":"2010-02-03T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.1101/cshperspect.a000539","status":"public","author":[{"first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"}],"scopus_import":"1","month":"02","article_type":"original","quality_controlled":"1","oa_version":"None","keyword":["General Biochemistry","Genetics and Molecular Biology"],"article_processing_charge":"No"},{"oa_version":"Published Version","quality_controlled":"1","article_type":"original","article_processing_charge":"No","keyword":["General Biochemistry","Genetics and Molecular Biology"],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2010.04.036"}],"month":"06","fulldoi":"https://doi.org/10.1016/j.cell.2010.04.036","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2010-06-11T00:00:00Z","scopus_import":"1","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","full_name":"HETZER, Martin W","first_name":"Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"oa":1,"date_created":"2022-04-07T07:53:29Z","extern":"1","day":"11","publication_status":"published","type":"journal_article","volume":141,"external_id":{"pmid":["20550937"]},"publisher":"Elsevier","language":[{"iso":"eng"}],"page":"1030-1041","_id":"11101","year":"2010","title":"Cell cycle-dependent differences in nuclear pore complex assembly in metazoa","publication":"Cell","doi":"10.1016/j.cell.2010.04.036","issue":"6","date_updated":"2024-10-14T11:28:00Z","intvolume":"       141","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>","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>.","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.","ista":"Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041.","chicago":"Doucet, Christine M., Jessica A. Talamas, and Martin Hetzer. “Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa.” <i>Cell</i>. Elsevier, 2010. <a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">https://doi.org/10.1016/j.cell.2010.04.036</a>.","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>","short":"C.M. Doucet, J.A. Talamas, M. Hetzer, Cell 141 (2010) 1030–1041."},"pmid":1,"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"}],"publication_identifier":{"issn":["0092-8674"]}},{"oa":1,"date_created":"2022-04-07T07:53:36Z","extern":"1","fulldoi":"https://doi.org/10.1016/j.cell.2009.12.054","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2010-02-05T00:00:00Z","scopus_import":"1","author":[{"first_name":"Maya","last_name":"Capelson","full_name":"Capelson, Maya"},{"first_name":"Yun","full_name":"Liang, Yun","last_name":"Liang"},{"first_name":"Roberta","last_name":"Schulte","full_name":"Schulte, Roberta"},{"first_name":"William","last_name":"Mair","full_name":"Mair, William"},{"last_name":"Wagner","full_name":"Wagner, Ulrich","first_name":"Ulrich"},{"orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W"}],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2009.12.054"}],"month":"02","oa_version":"Published Version","quality_controlled":"1","article_type":"original","keyword":["General Biochemistry","Genetics and Molecular Biology"],"article_processing_charge":"No","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."}],"publication_identifier":{"issn":["0092-8674"]},"doi":"10.1016/j.cell.2009.12.054","issue":"3","date_updated":"2024-10-14T11:28:14Z","intvolume":"       140","pmid":1,"citation":{"short":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, M. Hetzer, Cell 140 (2010) 372–383.","ama":"Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. <i>Cell</i>. 2010;140(3):372-383. doi:<a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">10.1016/j.cell.2009.12.054</a>","ista":"Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. 2010. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell. 140(3), 372–383.","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.","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>.","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>"},"volume":140,"external_id":{"pmid":["20144761"]},"publisher":"Elsevier","language":[{"iso":"eng"}],"page":"372-383","year":"2010","_id":"11102","title":"Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes","publication":"Cell","day":"05","publication_status":"published","type":"journal_article"},{"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."}],"publication_identifier":{"issn":["1534-5807"]},"issue":"5","date_updated":"2024-10-14T11:28:25Z","doi":"10.1016/j.devcel.2009.10.007","intvolume":"        17","citation":{"ieee":"M. Hetzer and S. R. Wente, “Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes,” <i>Developmental Cell</i>, vol. 17, no. 5. Elsevier, pp. 606–616, 2009.","ista":"Hetzer M, Wente SR. 2009. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. Developmental Cell. 17(5), 606–616.","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>.","short":"M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.","ama":"Hetzer M, Wente SR. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. <i>Developmental Cell</i>. 2009;17(5):606-616. doi:<a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">10.1016/j.devcel.2009.10.007</a>","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>","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>."},"pmid":1,"publisher":"Elsevier","volume":17,"external_id":{"pmid":["19922866"]},"title":"Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes","publication":"Developmental Cell","page":"606-616","language":[{"iso":"eng"}],"year":"2009","_id":"11103","publication_status":"published","day":"17","type":"journal_article","date_created":"2022-04-07T07:53:45Z","extern":"1","oa":1,"date_published":"2009-11-17T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","fulldoi":"https://doi.org/10.1016/j.devcel.2009.10.007","status":"public","scopus_import":"1","author":[{"full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"last_name":"Wente","full_name":"Wente, Susan R.","first_name":"Susan R."}],"main_file_link":[{"url":"https://doi.org/10.1016/j.devcel.2009.10.007","open_access":"1"}],"month":"11","article_type":"review","oa_version":"Published Version","quality_controlled":"1","article_processing_charge":"No","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"]},{"publication_identifier":{"issn":["0092-8674"]},"abstract":[{"lang":"eng","text":"In dividing cells, nuclear pore complexes (NPCs) disassemble during mitosis and reassemble into the newly forming nuclei. However, the fate of nuclear pores in postmitotic cells is unknown. Here, we show that NPCs, unlike other nuclear structures, do not turn over in differentiated cells. While a subset of NPC components, like Nup153 and Nup50, are continuously exchanged, scaffold nucleoporins, like the Nup107/160 complex, are extremely long-lived and remain incorporated in the nuclear membrane during the entire cellular life span. Besides the lack of nucleoporin expression and NPC turnover, we discovered an age-related deterioration of NPCs, leading to an increase in nuclear permeability and the leaking of cytoplasmic proteins into the nucleus. Our finding that nuclear “leakiness” is dramatically accelerated during aging and that a subset of nucleoporins is oxidatively damaged in old cells suggests that the accumulation of damage at the NPC might be a crucial aging event."}],"citation":{"apa":"D’Angelo, M. A., Raices, M., Panowski, S. H., &#38; Hetzer, M. (2009). Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">https://doi.org/10.1016/j.cell.2008.11.037</a>","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>.","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>.","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.","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.","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>","short":"M.A. D’Angelo, M. Raices, S.H. Panowski, M. Hetzer, Cell 136 (2009) 284–295."},"pmid":1,"intvolume":"       136","issue":"2","date_updated":"2024-10-14T11:28:59Z","doi":"10.1016/j.cell.2008.11.037","publication":"Cell","title":"Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells","year":"2009","_id":"11108","page":"284-295","language":[{"iso":"eng"}],"publisher":"Elsevier","external_id":{"pmid":["19167330"]},"volume":136,"type":"journal_article","publication_status":"published","day":"23","extern":"1","date_created":"2022-04-07T07:54:52Z","oa":1,"author":[{"first_name":"Maximiliano A.","last_name":"D'Angelo","full_name":"D'Angelo, Maximiliano A."},{"first_name":"Marcela","last_name":"Raices","full_name":"Raices, Marcela"},{"full_name":"Panowski, Siler H.","last_name":"Panowski","first_name":"Siler H."},{"last_name":"HETZER","full_name":"HETZER, Martin W","first_name":"Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"scopus_import":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2009-01-23T00:00:00Z","status":"public","fulldoi":"https://doi.org/10.1016/j.cell.2008.11.037","month":"01","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2008.11.037","open_access":"1"}],"article_processing_charge":"No","keyword":["General Biochemistry","Genetics and Molecular Biology"],"article_type":"original","quality_controlled":"1","oa_version":"Published Version"},{"issue":"2","date_updated":"2022-07-18T08:57:42Z","doi":"10.1016/s0092-8674(03)00235-6","pmid":1,"citation":{"ama":"Walther TC, Alves A, Pickersgill H, et al. The conserved Nup107-160 complex is critical for nuclear pore complex assembly. <i>Cell</i>. 2003;113(2):195-206. doi:<a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">10.1016/s0092-8674(03)00235-6</a>","short":"T.C. Walther, A. Alves, H. Pickersgill, I. Loı̈odice, M. Hetzer, V. Galy, B.B. Hülsmann, T. Köcher, M. Wilm, T. Allen, I.W. Mattaj, V. Doye, Cell 113 (2003) 195–206.","chicago":"Walther, Tobias C., Annabelle Alves, Helen Pickersgill, Isabelle Loı̈odice, Martin Hetzer, Vincent Galy, Bastian B. Hülsmann, et al. “The Conserved Nup107-160 Complex Is Critical for Nuclear Pore Complex Assembly.” <i>Cell</i>. Elsevier, 2003. <a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">https://doi.org/10.1016/s0092-8674(03)00235-6</a>.","ista":"Walther TC, Alves A, Pickersgill H, Loı̈odice I, Hetzer M, Galy V, Hülsmann BB, Köcher T, Wilm M, Allen T, Mattaj IW, Doye V. 2003. The conserved Nup107-160 complex is critical for nuclear pore complex assembly. Cell. 113(2), 195–206.","ieee":"T. C. Walther <i>et al.</i>, “The conserved Nup107-160 complex is critical for nuclear pore complex assembly,” <i>Cell</i>, vol. 113, no. 2. Elsevier, pp. 195–206, 2003.","mla":"Walther, Tobias C., et al. “The Conserved Nup107-160 Complex Is Critical for Nuclear Pore Complex Assembly.” <i>Cell</i>, vol. 113, no. 2, Elsevier, 2003, pp. 195–206, doi:<a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">10.1016/s0092-8674(03)00235-6</a>.","apa":"Walther, T. C., Alves, A., Pickersgill, H., Loı̈odice, I., Hetzer, M., Galy, V., … Doye, V. (2003). The conserved Nup107-160 complex is critical for nuclear pore complex assembly. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">https://doi.org/10.1016/s0092-8674(03)00235-6</a>"},"intvolume":"       113","abstract":[{"text":"Nuclear pore complexes (NPCs) are large multiprotein assemblies that allow traffic between the cytoplasm and the nucleus. During mitosis in higher eukaryotes, the Nuclear Envelope (NE) breaks down and NPCs disassemble. How NPCs reassemble and incorporate into the NE upon mitotic exit is poorly understood. We demonstrate a function for the conserved Nup107-160 complex in this process. Partial in vivo depletion of Nup133 or Nup107 via RNAi in HeLa cells resulted in reduced levels of multiple nucleoporins and decreased NPC density in the NE. Immunodepletion of the entire Nup107-160 complex from in vitro nuclear assembly reactions produced nuclei with a continuous NE but no NPCs. This phenotype was reversible only if Nup107-160 complex was readded before closed NE formation. Depletion also prevented association of FG-repeat nucleoporins with chromatin. We propose a stepwise model in which postmitotic NPC assembly initiates on chromatin via early recruitment of the Nup107-160 complex.","lang":"eng"}],"publication_identifier":{"issn":["0092-8674"]},"publication_status":"published","day":"17","type":"journal_article","publisher":"Elsevier","external_id":{"pmid":["12705868"]},"volume":113,"publication":"Cell","title":"The conserved Nup107-160 complex is critical for nuclear pore complex assembly","year":"2003","_id":"11122","language":[{"iso":"eng"}],"page":"195-206","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","date_published":"2003-04-17T00:00:00Z","fulldoi":"https://doi.org/10.1016/s0092-8674(03)00235-6","status":"public","author":[{"first_name":"Tobias C.","full_name":"Walther, Tobias C.","last_name":"Walther"},{"last_name":"Alves","full_name":"Alves, Annabelle","first_name":"Annabelle"},{"first_name":"Helen","full_name":"Pickersgill, Helen","last_name":"Pickersgill"},{"first_name":"Isabelle","last_name":"Loı̈odice","full_name":"Loı̈odice, Isabelle"},{"first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"},{"first_name":"Vincent","full_name":"Galy, Vincent","last_name":"Galy"},{"first_name":"Bastian B.","last_name":"Hülsmann","full_name":"Hülsmann, Bastian B."},{"first_name":"Thomas","last_name":"Köcher","full_name":"Köcher, Thomas"},{"last_name":"Wilm","full_name":"Wilm, Matthias","first_name":"Matthias"},{"first_name":"Terry","last_name":"Allen","full_name":"Allen, Terry"},{"last_name":"Mattaj","full_name":"Mattaj, Iain W.","first_name":"Iain W."},{"last_name":"Doye","full_name":"Doye, Valérie","first_name":"Valérie"}],"scopus_import":"1","extern":"1","date_created":"2022-04-07T07:57:10Z","article_type":"original","quality_controlled":"1","oa_version":"Published Version","article_processing_charge":"No","keyword":["General Biochemistry","Genetics and Molecular Biology"],"month":"04"},{"main_file_link":[{"url":"https://doi.org/10.1016/S0960-9822(02)00927-2","open_access":"1"}],"month":"07","article_type":"letter_note","oa_version":"Published Version","quality_controlled":"1","article_processing_charge":"No","keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"date_created":"2022-04-07T07:57:31Z","extern":"1","oa":1,"date_published":"2002-07-09T00:00:00Z","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","fulldoi":"https://doi.org/10.1016/s0960-9822(02)00927-2","scopus_import":"1","author":[{"last_name":"Bilbao-Cortés","full_name":"Bilbao-Cortés, Daniel","first_name":"Daniel"},{"first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"},{"first_name":"Gernot","last_name":"Längst","full_name":"Längst, Gernot"},{"last_name":"Becker","full_name":"Becker, Peter B.","first_name":"Peter B."},{"first_name":"Iain W.","full_name":"Mattaj, Iain W.","last_name":"Mattaj"}],"publisher":"Elsevier BV","volume":12,"external_id":{"pmid":["12121625"]},"title":"Ran binds to chromatin by two distinct mechanisms","publication":"Current Biology","page":"1151-1156","language":[{"iso":"eng"}],"year":"2002","_id":"11124","publication_status":"published","day":"09","type":"journal_article","abstract":[{"text":"Ran GTPase plays important roles in nucleocytoplasmic transport in interphase [1, 2] and in both spindle formation and nuclear envelope (NE) assembly during mitosis [3, 4, 5]. The latter functions rely on the presence of high local concentrations of GTP-bound Ran near mitotic chromatin [3, 4, 5]. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin [6, 7, 8, 9], but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes. We propose that the Ran binding capacity of chromatin contributes to localized spindle and NE assembly.","lang":"eng"}],"publication_identifier":{"issn":["0960-9822"]},"issue":"13","date_updated":"2022-07-18T08:58:05Z","doi":"10.1016/s0960-9822(02)00927-2","intvolume":"        12","citation":{"ieee":"D. Bilbao-Cortés, M. Hetzer, G. Längst, P. B. Becker, and I. W. Mattaj, “Ran binds to chromatin by two distinct mechanisms,” <i>Current Biology</i>, vol. 12, no. 13. Elsevier BV, pp. 1151–1156, 2002.","ista":"Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. 2002. Ran binds to chromatin by two distinct mechanisms. Current Biology. 12(13), 1151–1156.","chicago":"Bilbao-Cortés, Daniel, Martin Hetzer, Gernot Längst, Peter B. Becker, and Iain W. Mattaj. “Ran Binds to Chromatin by Two Distinct Mechanisms.” <i>Current Biology</i>. Elsevier BV, 2002. <a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">https://doi.org/10.1016/s0960-9822(02)00927-2</a>.","short":"D. Bilbao-Cortés, M. Hetzer, G. Längst, P.B. Becker, I.W. Mattaj, Current Biology 12 (2002) 1151–1156.","ama":"Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. Ran binds to chromatin by two distinct mechanisms. <i>Current Biology</i>. 2002;12(13):1151-1156. doi:<a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">10.1016/s0960-9822(02)00927-2</a>","apa":"Bilbao-Cortés, D., Hetzer, M., Längst, G., Becker, P. B., &#38; Mattaj, I. W. (2002). Ran binds to chromatin by two distinct mechanisms. <i>Current Biology</i>. Elsevier BV. <a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">https://doi.org/10.1016/s0960-9822(02)00927-2</a>","mla":"Bilbao-Cortés, Daniel, et al. “Ran Binds to Chromatin by Two Distinct Mechanisms.” <i>Current Biology</i>, vol. 12, no. 13, Elsevier BV, 2002, pp. 1151–56, doi:<a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">10.1016/s0960-9822(02)00927-2</a>."},"pmid":1}]