[{"type":"journal_article","day":"01","status":"public","intvolume":"         3","page":"88-100","publication":"Nucleus","issue":"1","date_published":"2012-01-01T00:00:00Z","article_type":"original","month":"01","language":[{"iso":"eng"}],"scopus_import":"1","publisher":"Taylor & Francis","date_created":"2022-04-07T07:51:53Z","citation":{"chicago":"Vargas, Jesse D., Emily M. Hatch, Daniel J. Anderson, and Martin Hetzer. “Transient Nuclear Envelope Rupturing during Interphase in Human Cancer Cells.” <i>Nucleus</i>. Taylor &#38; Francis, 2012. <a href=\"https://doi.org/10.4161/nucl.18954\">https://doi.org/10.4161/nucl.18954</a>.","apa":"Vargas, J. D., Hatch, E. M., Anderson, D. J., &#38; Hetzer, M. (2012). Transient nuclear envelope rupturing during interphase in human cancer cells. <i>Nucleus</i>. Taylor &#38; Francis. <a href=\"https://doi.org/10.4161/nucl.18954\">https://doi.org/10.4161/nucl.18954</a>","ieee":"J. D. Vargas, E. M. Hatch, D. J. Anderson, and M. Hetzer, “Transient nuclear envelope rupturing during interphase in human cancer cells,” <i>Nucleus</i>, vol. 3, no. 1. Taylor &#38; Francis, pp. 88–100, 2012.","short":"J.D. Vargas, E.M. Hatch, D.J. Anderson, M. Hetzer, Nucleus 3 (2012) 88–100.","ista":"Vargas JD, Hatch EM, Anderson DJ, Hetzer M. 2012. Transient nuclear envelope rupturing during interphase in human cancer cells. Nucleus. 3(1), 88–100.","ama":"Vargas JD, Hatch EM, Anderson DJ, Hetzer M. Transient nuclear envelope rupturing during interphase in human cancer cells. <i>Nucleus</i>. 2012;3(1):88-100. doi:<a href=\"https://doi.org/10.4161/nucl.18954\">10.4161/nucl.18954</a>","mla":"Vargas, Jesse D., et al. “Transient Nuclear Envelope Rupturing during Interphase in Human Cancer Cells.” <i>Nucleus</i>, vol. 3, no. 1, Taylor &#38; Francis, 2012, pp. 88–100, doi:<a href=\"https://doi.org/10.4161/nucl.18954\">10.4161/nucl.18954</a>."},"publication_status":"published","author":[{"first_name":"Jesse D.","last_name":"Vargas","full_name":"Vargas, Jesse D."},{"last_name":"Hatch","full_name":"Hatch, Emily M.","first_name":"Emily M."},{"full_name":"Anderson, Daniel J.","last_name":"Anderson","first_name":"Daniel J."},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"keyword":["Cell Biology"],"abstract":[{"lang":"eng","text":"Neoplastic cells are often characterized by specific morphological abnormalities of the nuclear envelope (NE), which have been used for cancer diagnosis for more than a century. The NE is a double phospholipid bilayer that encapsulates the nuclear genome, regulates all nuclear trafficking of RNAs and proteins and prevents the passive diffusion of macromolecules between the nucleoplasm and the cytoplasm. Whether there is a consequence to the proper functioning of the cell and loss of structural integrity of the nucleus remains unclear. Using live cell imaging, we characterize a phenomenon wherein nuclei of several proliferating human cancer cell lines become temporarily ruptured during interphase. Strikingly, NE rupturing was associated with the mislocalization of nucleoplasmic and cytoplasmic proteins and, in the most extreme cases, the entrapment of cytoplasmic organelles in the nuclear interior. In addition, we observed the formation of micronuclei-like structures during interphase and the movement of chromatin out of the nuclear space. The frequency of these NE rupturing events was higher in cells in which the nuclear lamina, a network of intermediate filaments providing mechanical support to the NE, was not properly formed. Our data uncover the existence of a NE instability that has the potential to change the genomic landscape of cancer cells."}],"article_processing_charge":"No","date_updated":"2022-07-18T08:52:53Z","volume":3,"quality_controlled":"1","oa_version":"None","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication_identifier":{"issn":["1949-1034"],"eissn":["1949-1042"]},"extern":"1","_id":"11091","pmid":1,"doi":"10.4161/nucl.18954","year":"2012","external_id":{"pmid":["22567193"]},"title":"Transient nuclear envelope rupturing during interphase in human cancer cells"},{"publisher":"Elsevier","scopus_import":"1","language":[{"iso":"eng"}],"month":"01","date_published":"2012-01-19T00:00:00Z","article_type":"original","date_created":"2022-04-07T07:52:10Z","intvolume":"        22","status":"public","day":"19","type":"journal_article","issue":"2","publication":"Developmental Cell","page":"446-458","title":"A change in nuclear pore complex composition regulates cell differentiation","external_id":{"pmid":["22264802"]},"doi":"10.1016/j.devcel.2011.11.021","year":"2012","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2011.11.021"}],"abstract":[{"lang":"eng","text":"Nuclear pore complexes (NPCs) are built from ∼30 different proteins called nucleoporins or Nups. Previous studies have shown that several Nups exhibit cell-type-specific expression and that mutations in NPC components result in tissue-specific diseases. Here we show that a specific change in NPC composition is required for both myogenic and neuronal differentiation. The transmembrane nucleoporin Nup210 is absent in proliferating myoblasts and embryonic stem cells (ESCs) but becomes expressed and incorporated into NPCs during cell differentiation. Preventing Nup210 production by RNAi blocks myogenesis and the differentiation of ESCs into neuroprogenitors. We found that the addition of Nup210 to NPCs does not affect nuclear transport but is required for the induction of genes that are essential for cell differentiation. Our results identify a single change in NPC composition as an essential step in cell differentiation and establish a role for Nup210 in gene expression regulation and cell fate determination."}],"author":[{"first_name":"Maximiliano A.","full_name":"D'Angelo, Maximiliano A.","last_name":"D'Angelo"},{"first_name":"J. Sebastian","full_name":"Gomez-Cavazos, J. Sebastian","last_name":"Gomez-Cavazos"},{"full_name":"Mei, Arianna","last_name":"Mei","first_name":"Arianna"},{"full_name":"Lackner, Daniel H.","last_name":"Lackner","first_name":"Daniel H."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","first_name":"Martin W"}],"keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"publication_status":"published","citation":{"short":"M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental Cell 22 (2012) 446–458.","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>","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.","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>"},"_id":"11093","pmid":1,"extern":"1","publication_identifier":{"issn":["1534-5807"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","quality_controlled":"1","oa_version":"Published Version","oa":1,"date_updated":"2022-07-18T08:53:16Z","volume":22,"article_processing_charge":"No"},{"date_created":"2022-04-07T07:52:18Z","month":"07","date_published":"2011-07-04T00:00:00Z","article_type":"original","scopus_import":"1","publisher":"Rockefeller University Press","language":[{"iso":"eng"}],"publication":"Journal of Cell Biology","issue":"1","page":"27-37","day":"04","type":"journal_article","intvolume":"       194","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.201012154"}],"doi":"10.1083/jcb.201012154","year":"2011","title":"POM121 and Sun1 play a role in early steps of interphase NPC assembly","external_id":{"pmid":["21727197"]},"article_processing_charge":"No","date_updated":"2022-07-18T08:53:46Z","oa":1,"volume":194,"extern":"1","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"_id":"11094","pmid":1,"quality_controlled":"1","oa_version":"Published Version","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"apa":"Talamas, J. A., &#38; Hetzer, M. (2011). POM121 and Sun1 play a role in early steps of interphase NPC assembly. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201012154\">https://doi.org/10.1083/jcb.201012154</a>","ieee":"J. A. Talamas and M. Hetzer, “POM121 and Sun1 play a role in early steps of interphase NPC assembly,” <i>Journal of Cell Biology</i>, vol. 194, no. 1. Rockefeller University Press, pp. 27–37, 2011.","chicago":"Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in Early Steps of Interphase NPC Assembly.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2011. <a href=\"https://doi.org/10.1083/jcb.201012154\">https://doi.org/10.1083/jcb.201012154</a>.","ama":"Talamas JA, Hetzer M. POM121 and Sun1 play a role in early steps of interphase NPC assembly. <i>Journal of Cell Biology</i>. 2011;194(1):27-37. doi:<a href=\"https://doi.org/10.1083/jcb.201012154\">10.1083/jcb.201012154</a>","mla":"Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in Early Steps of Interphase NPC Assembly.” <i>Journal of Cell Biology</i>, vol. 194, no. 1, Rockefeller University Press, 2011, pp. 27–37, doi:<a href=\"https://doi.org/10.1083/jcb.201012154\">10.1083/jcb.201012154</a>.","ista":"Talamas JA, Hetzer M. 2011. POM121 and Sun1 play a role in early steps of interphase NPC assembly. Journal of Cell Biology. 194(1), 27–37.","short":"J.A. Talamas, M. Hetzer, Journal of Cell Biology 194 (2011) 27–37."},"publication_status":"published","abstract":[{"lang":"eng","text":"Nuclear pore complexes (NPCs) assemble at the end of mitosis during nuclear envelope (NE) reformation and into an intact NE as cells progress through interphase. Although recent studies have shown that NPC formation occurs by two different molecular mechanisms at two distinct cell cycle stages, little is known about the molecular players that mediate the fusion of the outer and inner nuclear membranes to form pores. In this paper, we provide evidence that the transmembrane nucleoporin (Nup), POM121, but not the Nup107–160 complex, is present at new pore assembly sites at a time that coincides with inner nuclear membrane (INM) and outer nuclear membrane (ONM) fusion. Overexpression of POM121 resulted in juxtaposition of the INM and ONM. Additionally, Sun1, an INM protein that is known to interact with the cytoskeleton, was specifically required for interphase assembly and localized with POM121 at forming pores. We propose a model in which POM121 and Sun1 interact transiently to promote early steps of interphase NPC assembly."}],"author":[{"first_name":"Jessica A.","last_name":"Talamas","full_name":"Talamas, Jessica A."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","first_name":"Martin W"}],"keyword":["Cell Biology"]},{"publication_status":"published","citation":{"apa":"Hetzer, M., &#38; Cavalli, G. (2011). Editorial overview. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">https://doi.org/10.1016/j.ceb.2011.04.013</a>","ieee":"M. Hetzer and G. Cavalli, “Editorial overview,” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 3. Elsevier, pp. 255–257, 2011.","chicago":"Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2011. <a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">https://doi.org/10.1016/j.ceb.2011.04.013</a>.","ama":"Hetzer M, Cavalli G. Editorial overview. <i>Current Opinion in Cell Biology</i>. 2011;23(3):255-257. doi:<a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">10.1016/j.ceb.2011.04.013</a>","mla":"Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 3, Elsevier, 2011, pp. 255–57, doi:<a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">10.1016/j.ceb.2011.04.013</a>.","ista":"Hetzer M, Cavalli G. 2011. Editorial overview. Current Opinion in Cell Biology. 23(3), 255–257.","short":"M. Hetzer, G. Cavalli, Current Opinion in Cell Biology 23 (2011) 255–257."},"author":[{"first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"full_name":"Cavalli, Giacomo","last_name":"Cavalli","first_name":"Giacomo"}],"keyword":["Cell Biology"],"date_updated":"2022-07-18T08:39:40Z","volume":23,"article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","quality_controlled":"1","oa_version":"None","_id":"11095","pmid":1,"publication_identifier":{"issn":["0955-0674"]},"extern":"1","doi":"10.1016/j.ceb.2011.04.013","year":"2011","external_id":{"pmid":["21592757"]},"title":"Editorial overview","type":"journal_article","day":"01","status":"public","intvolume":"        23","page":"255-257","issue":"3","publication":"Current Opinion in Cell Biology","article_type":"letter_note","date_published":"2011-06-01T00:00:00Z","month":"06","language":[{"iso":"eng"}],"publisher":"Elsevier","scopus_import":"1","date_created":"2022-04-07T07:52:27Z"},{"day":"01","type":"journal_article","intvolume":"        23","status":"public","issue":"1","publication":"Current Opinion in Cell Biology","page":"65-70","month":"02","date_published":"2011-02-01T00:00:00Z","article_type":"original","publisher":"Elsevier","scopus_import":"1","language":[{"iso":"eng"}],"date_created":"2022-04-07T07:52:37Z","publication_status":"published","citation":{"short":"Y. Liang, M. Hetzer, Current Opinion in Cell Biology 23 (2011) 65–70.","ista":"Liang Y, Hetzer M. 2011. Functional interactions between nucleoporins and chromatin. Current Opinion in Cell Biology. 23(1), 65–70.","ama":"Liang Y, Hetzer M. Functional interactions between nucleoporins and chromatin. <i>Current Opinion in Cell Biology</i>. 2011;23(1):65-70. doi:<a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">10.1016/j.ceb.2010.09.008</a>","mla":"Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins and Chromatin.” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 1, Elsevier, 2011, pp. 65–70, doi:<a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">10.1016/j.ceb.2010.09.008</a>.","chicago":"Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins and Chromatin.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2011. <a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">https://doi.org/10.1016/j.ceb.2010.09.008</a>.","ieee":"Y. Liang and M. Hetzer, “Functional interactions between nucleoporins and chromatin,” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 1. Elsevier, pp. 65–70, 2011.","apa":"Liang, Y., &#38; Hetzer, M. (2011). Functional interactions between nucleoporins and chromatin. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">https://doi.org/10.1016/j.ceb.2010.09.008</a>"},"abstract":[{"lang":"eng","text":"As the gatekeepers of the eukaryotic cell nucleus, nuclear pore complexes (NPCs) mediate all molecular trafficking between the nucleoplasm and the cytoplasm. In recent years, transport-independent functions of NPC components, nucleoporins, have been identified including roles in chromatin organization and gene regulation. Here, we summarize our current view of the NPC as a dynamic hub for the integration of chromatin regulation and nuclear trafficking and discuss the functional interplay between nucleoporins and the nuclear genome."}],"keyword":["Cell Biology"],"author":[{"first_name":"Yun","full_name":"Liang, Yun","last_name":"Liang"},{"first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"volume":23,"date_updated":"2022-07-18T08:53:48Z","article_processing_charge":"No","_id":"11096","pmid":1,"publication_identifier":{"issn":["0955-0674"]},"extern":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa_version":"None","quality_controlled":"1","year":"2011","doi":"10.1016/j.ceb.2010.09.008","external_id":{"pmid":["21030234"]},"title":"Functional interactions between nucleoporins and chromatin"},{"doi":"10.18632/aging.100125","year":"2010","title":"The role of the nuclear pore complex in aging of post-mitotic cells","external_id":{"pmid":["20354266"]},"main_file_link":[{"url":"https://doi.org/10.18632/aging.100125","open_access":"1"}],"publication_status":"published","citation":{"apa":"Hetzer, M. (2010). The role of the nuclear pore complex in aging of post-mitotic cells. <i>Aging</i>. Impact Journals. <a href=\"https://doi.org/10.18632/aging.100125\">https://doi.org/10.18632/aging.100125</a>","ieee":"M. Hetzer, “The role of the nuclear pore complex in aging of post-mitotic cells,” <i>Aging</i>, vol. 2, no. 2. Impact Journals, pp. 74–75, 2010.","chicago":"Hetzer, Martin. “The Role of the Nuclear Pore Complex in Aging of Post-Mitotic Cells.” <i>Aging</i>. Impact Journals, 2010. <a href=\"https://doi.org/10.18632/aging.100125\">https://doi.org/10.18632/aging.100125</a>.","ama":"Hetzer M. The role of the nuclear pore complex in aging of post-mitotic cells. <i>Aging</i>. 2010;2(2):74-75. doi:<a href=\"https://doi.org/10.18632/aging.100125\">10.18632/aging.100125</a>","mla":"Hetzer, Martin. “The Role of the Nuclear Pore Complex in Aging of Post-Mitotic Cells.” <i>Aging</i>, vol. 2, no. 2, Impact Journals, 2010, pp. 74–75, doi:<a href=\"https://doi.org/10.18632/aging.100125\">10.18632/aging.100125</a>.","ista":"Hetzer M. 2010. The role of the nuclear pore complex in aging of post-mitotic cells. Aging. 2(2), 74–75.","short":"M. Hetzer, Aging 2 (2010) 74–75."},"keyword":["Cell Biology","Aging"],"author":[{"first_name":"Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"date_updated":"2022-07-18T08:54:15Z","volume":2,"oa":1,"article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa_version":"Published Version","quality_controlled":"1","pmid":1,"_id":"11098","extern":"1","publication_identifier":{"issn":["1945-4589"]},"date_published":"2010-02-01T00:00:00Z","article_type":"original","month":"02","language":[{"iso":"eng"}],"publisher":"Impact Journals","scopus_import":"1","date_created":"2022-04-07T07:52:58Z","type":"journal_article","day":"01","status":"public","intvolume":"         2","page":"74-75","issue":"2","publication":"Aging"},{"publication":"Journal of Biological Chemistry","issue":"8","article_processing_charge":"No","page":"5827-5835","date_updated":"2021-01-12T08:19:31Z","volume":285,"publication_identifier":{"issn":["0021-9258","1083-351X"]},"extern":"1","_id":"8473","quality_controlled":"1","oa_version":"None","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","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>.","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>","ieee":"A. Corazza <i>et al.</i>, “Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR,” <i>Journal of Biological Chemistry</i>, vol. 285, no. 8. American Society for Biochemistry &#38; Molecular Biology, pp. 5827–5835, 2010.","short":"A. Corazza, E. Rennella, P. Schanda, M.C. Mimmi, T. Cutuil, S. Raimondi, S. Giorgetti, F. Fogolari, P. Viglino, L. Frydman, M. Gal, V. Bellotti, B. Brutscher, G. Esposito, Journal of Biological Chemistry 285 (2010) 5827–5835.","ista":"Corazza A, Rennella E, Schanda P, Mimmi MC, Cutuil T, Raimondi S, Giorgetti S, Fogolari F, Viglino P, Frydman L, Gal M, Bellotti V, Brutscher B, Esposito G. 2010. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. Journal of Biological Chemistry. 285(8), 5827–5835.","mla":"Corazza, Alessandra, et al. “Native-Unlike Long-Lived Intermediates along the Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin Revealed by Real-Time Two-Dimensional NMR.” <i>Journal of Biological Chemistry</i>, vol. 285, no. 8, American Society for Biochemistry &#38; Molecular Biology, 2010, pp. 5827–35, doi:<a href=\"https://doi.org/10.1074/jbc.m109.061168\">10.1074/jbc.m109.061168</a>.","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>"},"day":"19","publication_status":"published","type":"journal_article","intvolume":"       285","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."}],"keyword":["Cell Biology","Biochemistry","Molecular Biology"],"status":"public","author":[{"last_name":"Corazza","full_name":"Corazza, Alessandra","first_name":"Alessandra"},{"first_name":"Enrico","last_name":"Rennella","full_name":"Rennella, Enrico"},{"full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"full_name":"Mimmi, Maria Chiara","last_name":"Mimmi","first_name":"Maria Chiara"},{"first_name":"Thomas","last_name":"Cutuil","full_name":"Cutuil, Thomas"},{"full_name":"Raimondi, Sara","last_name":"Raimondi","first_name":"Sara"},{"first_name":"Sofia","full_name":"Giorgetti, Sofia","last_name":"Giorgetti"},{"first_name":"Federico","full_name":"Fogolari, Federico","last_name":"Fogolari"},{"first_name":"Paolo","last_name":"Viglino","full_name":"Viglino, Paolo"},{"full_name":"Frydman, Lucio","last_name":"Frydman","first_name":"Lucio"},{"first_name":"Maayan","last_name":"Gal","full_name":"Gal, Maayan"},{"full_name":"Bellotti, Vittorio","last_name":"Bellotti","first_name":"Vittorio"},{"full_name":"Brutscher, Bernhard","last_name":"Brutscher","first_name":"Bernhard"},{"full_name":"Esposito, Gennaro","last_name":"Esposito","first_name":"Gennaro"}],"date_created":"2020-09-18T10:11:23Z","year":"2010","doi":"10.1074/jbc.m109.061168","month":"02","date_published":"2010-02-19T00:00:00Z","article_type":"original","title":"Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR","publisher":"American Society for Biochemistry & Molecular Biology","language":[{"iso":"eng"}]},{"intvolume":"        17","status":"public","day":"17","type":"journal_article","publication":"Developmental Cell","issue":"5","page":"606-616","scopus_import":"1","publisher":"Elsevier","language":[{"iso":"eng"}],"month":"11","date_published":"2009-11-17T00:00:00Z","article_type":"review","date_created":"2022-04-07T07:53:45Z","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."}],"keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"author":[{"first_name":"Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"last_name":"Wente","full_name":"Wente, Susan R.","first_name":"Susan R."}],"citation":{"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>.","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>","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.","short":"M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.","apa":"Hetzer, M., &#38; Wente, S. R. (2009). Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. <i>Developmental Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">https://doi.org/10.1016/j.devcel.2009.10.007</a>","ieee":"M. Hetzer and S. R. Wente, “Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes,” <i>Developmental Cell</i>, vol. 17, no. 5. Elsevier, pp. 606–616, 2009.","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>."},"publication_status":"published","extern":"1","publication_identifier":{"issn":["1534-5807"]},"_id":"11103","pmid":1,"quality_controlled":"1","oa_version":"Published Version","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","volume":17,"oa":1,"date_updated":"2022-07-18T08:55:01Z","external_id":{"pmid":["19922866"]},"title":"Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes","doi":"10.1016/j.devcel.2009.10.007","year":"2009","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2009.10.007"}]},{"page":"183-191","publication":"Journal of Cell Biology","issue":"2","type":"journal_article","day":"20","status":"public","intvolume":"       186","date_created":"2022-04-07T07:54:18Z","article_type":"original","date_published":"2009-07-20T00:00:00Z","month":"07","language":[{"iso":"eng"}],"scopus_import":"1","publisher":"Rockefeller University Press","article_processing_charge":"No","volume":186,"date_updated":"2022-07-18T08:58:35Z","oa":1,"quality_controlled":"1","oa_version":"Published Version","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"extern":"1","_id":"11106","pmid":1,"citation":{"ieee":"D. J. Anderson, J. D. Vargas, J. P. Hsiao, and M. Hetzer, “Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo,” <i>Journal of Cell Biology</i>, vol. 186, no. 2. Rockefeller University Press, pp. 183–191, 2009.","apa":"Anderson, D. J., Vargas, J. D., Hsiao, J. P., &#38; Hetzer, M. (2009). Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.200901106\">https://doi.org/10.1083/jcb.200901106</a>","chicago":"Anderson, Daniel J., Jesse D. Vargas, Joshua P. Hsiao, and Martin Hetzer. “Recruitment of Functionally Distinct Membrane Proteins to Chromatin Mediates Nuclear Envelope Formation in Vivo.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2009. <a href=\"https://doi.org/10.1083/jcb.200901106\">https://doi.org/10.1083/jcb.200901106</a>.","mla":"Anderson, Daniel J., et al. “Recruitment of Functionally Distinct Membrane Proteins to Chromatin Mediates Nuclear Envelope Formation in Vivo.” <i>Journal of Cell Biology</i>, vol. 186, no. 2, Rockefeller University Press, 2009, pp. 183–91, doi:<a href=\"https://doi.org/10.1083/jcb.200901106\">10.1083/jcb.200901106</a>.","ama":"Anderson DJ, Vargas JD, Hsiao JP, Hetzer M. Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. <i>Journal of Cell Biology</i>. 2009;186(2):183-191. doi:<a href=\"https://doi.org/10.1083/jcb.200901106\">10.1083/jcb.200901106</a>","ista":"Anderson DJ, Vargas JD, Hsiao JP, Hetzer M. 2009. Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. Journal of Cell Biology. 186(2), 183–191.","short":"D.J. Anderson, J.D. Vargas, J.P. Hsiao, M. Hetzer, Journal of Cell Biology 186 (2009) 183–191."},"publication_status":"published","keyword":["Cell Biology"],"author":[{"last_name":"Anderson","full_name":"Anderson, Daniel J.","first_name":"Daniel J."},{"first_name":"Jesse D.","full_name":"Vargas, Jesse D.","last_name":"Vargas"},{"first_name":"Joshua P.","full_name":"Hsiao, Joshua P.","last_name":"Hsiao"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X"}],"abstract":[{"text":"Formation of the nuclear envelope (NE) around segregated chromosomes occurs by the reshaping of the endoplasmic reticulum (ER), a reservoir for disassembled nuclear membrane components during mitosis. In this study, we show that inner nuclear membrane proteins such as lamin B receptor (LBR), MAN1, Lap2β, and the trans-membrane nucleoporins Ndc1 and POM121 drive the spreading of ER membranes into the emerging NE via their capacity to bind chromatin in a collaborative manner. Despite their redundant functions, decreasing the levels of any of these trans-membrane proteins by RNAi-mediated knockdown delayed NE formation, whereas increasing the levels of any of them had the opposite effect. Furthermore, acceleration of NE formation interferes with chromosome separation during mitosis, indicating that the time frame over which chromatin becomes membrane enclosed is physiologically relevant and regulated. These data suggest that functionally distinct classes of chromatin-interacting membrane proteins, which are present at nonsaturating levels, collaborate to rapidly reestablish the nuclear compartment at the end of mitosis.","lang":"eng"}],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.200901106"}],"related_material":{"link":[{"url":"https://doi.org/10.1083/jcb.20090110620090903c","relation":"erratum"}]},"year":"2009","doi":"10.1083/jcb.200901106","title":"Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo","external_id":{"pmid":["19620630"]}},{"main_file_link":[{"url":"https://doi.org/10.1083/jcb.200806174","open_access":"1"}],"doi":"10.1083/jcb.200806174","year":"2009","external_id":{"pmid":["19273614"]},"title":"ER membrane–bending proteins are necessary for de novo nuclear pore formation","article_processing_charge":"No","volume":184,"date_updated":"2022-07-18T08:55:05Z","oa":1,"quality_controlled":"1","oa_version":"Published Version","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","extern":"1","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"pmid":1,"_id":"11107","citation":{"apa":"Dawson, T. R., Lazarus, M. D., Hetzer, M., &#38; Wente, S. R. (2009). ER membrane–bending proteins are necessary for de novo nuclear pore formation. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.200806174\">https://doi.org/10.1083/jcb.200806174</a>","ieee":"T. R. Dawson, M. D. Lazarus, M. Hetzer, and S. R. Wente, “ER membrane–bending proteins are necessary for de novo nuclear pore formation,” <i>Journal of Cell Biology</i>, vol. 184, no. 5. Rockefeller University Press, pp. 659–675, 2009.","chicago":"Dawson, T. Renee, Michelle D. Lazarus, Martin Hetzer, and Susan R. Wente. “ER Membrane–Bending Proteins Are Necessary for de Novo Nuclear Pore Formation.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2009. <a href=\"https://doi.org/10.1083/jcb.200806174\">https://doi.org/10.1083/jcb.200806174</a>.","mla":"Dawson, T. Renee, et al. “ER Membrane–Bending Proteins Are Necessary for de Novo Nuclear Pore Formation.” <i>Journal of Cell Biology</i>, vol. 184, no. 5, Rockefeller University Press, 2009, pp. 659–75, doi:<a href=\"https://doi.org/10.1083/jcb.200806174\">10.1083/jcb.200806174</a>.","ama":"Dawson TR, Lazarus MD, Hetzer M, Wente SR. ER membrane–bending proteins are necessary for de novo nuclear pore formation. <i>Journal of Cell Biology</i>. 2009;184(5):659-675. doi:<a href=\"https://doi.org/10.1083/jcb.200806174\">10.1083/jcb.200806174</a>","ista":"Dawson TR, Lazarus MD, Hetzer M, Wente SR. 2009. ER membrane–bending proteins are necessary for de novo nuclear pore formation. Journal of Cell Biology. 184(5), 659–675.","short":"T.R. Dawson, M.D. Lazarus, M. Hetzer, S.R. Wente, Journal of Cell Biology 184 (2009) 659–675."},"publication_status":"published","keyword":["Cell Biology"],"author":[{"first_name":"T. Renee","full_name":"Dawson, T. Renee","last_name":"Dawson"},{"first_name":"Michelle D.","last_name":"Lazarus","full_name":"Lazarus, Michelle D."},{"orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"first_name":"Susan R.","full_name":"Wente, Susan R.","last_name":"Wente"}],"abstract":[{"text":"Nucleocytoplasmic transport occurs exclusively through nuclear pore complexes (NPCs) embedded in pores formed by inner and outer nuclear membrane fusion. The mechanism for de novo pore and NPC biogenesis remains unclear. Reticulons (RTNs) and Yop1/DP1 are conserved membrane protein families required to form and maintain the tubular endoplasmic reticulum (ER) and the postmitotic nuclear envelope. In this study, we report that members of the RTN and Yop1/DP1 families are required for nuclear pore formation. Analysis of Saccharomyces cerevisiae prp20-G282S and nup133Δ NPC assembly mutants revealed perturbations in Rtn1–green fluorescent protein (GFP) and Yop1-GFP ER distribution and colocalization to NPC clusters. Combined deletion of RTN1 and YOP1 resulted in NPC clustering, nuclear import defects, and synthetic lethality with the additional absence of Pom34, Pom152, and Nup84 subcomplex members. We tested for a direct role in NPC biogenesis using Xenopus laevis in vitro assays and found that anti-Rtn4a antibodies specifically inhibited de novo nuclear pore formation. We hypothesize that these ER membrane–bending proteins mediate early NPC assembly steps.","lang":"eng"}],"date_created":"2022-04-07T07:54:44Z","date_published":"2009-03-09T00:00:00Z","article_type":"original","month":"03","language":[{"iso":"eng"}],"scopus_import":"1","publisher":"Rockefeller University Press","page":"659-675","publication":"Journal of Cell Biology","issue":"5","type":"journal_article","day":"09","status":"public","intvolume":"       184"},{"publication_status":"published","citation":{"short":"U. Kutay, M. Hetzer, Current Opinion in Cell Biology 20 (2008) 669–677.","ista":"Kutay U, Hetzer M. 2008. Reorganization of the nuclear envelope during open mitosis. Current Opinion in Cell Biology. 20(6), 669–677.","mla":"Kutay, Ulrike, and Martin Hetzer. “Reorganization of the Nuclear Envelope during Open Mitosis.” <i>Current Opinion in Cell Biology</i>, vol. 20, no. 6, Elsevier, 2008, pp. 669–77, doi:<a href=\"https://doi.org/10.1016/j.ceb.2008.09.010\">10.1016/j.ceb.2008.09.010</a>.","ama":"Kutay U, Hetzer M. Reorganization of the nuclear envelope during open mitosis. <i>Current Opinion in Cell Biology</i>. 2008;20(6):669-677. doi:<a href=\"https://doi.org/10.1016/j.ceb.2008.09.010\">10.1016/j.ceb.2008.09.010</a>","chicago":"Kutay, Ulrike, and Martin Hetzer. “Reorganization of the Nuclear Envelope during Open Mitosis.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2008. <a href=\"https://doi.org/10.1016/j.ceb.2008.09.010\">https://doi.org/10.1016/j.ceb.2008.09.010</a>.","apa":"Kutay, U., &#38; Hetzer, M. (2008). Reorganization of the nuclear envelope during open mitosis. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2008.09.010\">https://doi.org/10.1016/j.ceb.2008.09.010</a>","ieee":"U. Kutay and M. Hetzer, “Reorganization of the nuclear envelope during open mitosis,” <i>Current Opinion in Cell Biology</i>, vol. 20, no. 6. Elsevier, pp. 669–677, 2008."},"abstract":[{"lang":"eng","text":"The nuclear envelope (NE) provides a selective barrier between the nuclear interior and the cytoplasm and constitutes a central component of intracellular architecture. During mitosis in metazoa, the NE breaks down leading to the complete mixing of the nuclear content with the cytosol. Interestingly, many NE components actively participate in mitotic progression. After chromosome segregation, the NE is reassembled around decondensing chromatin and the nuclear compartment is reestablished in the daughter cells. Here, we summarize recent progress in deciphering the molecular mechanisms underlying NE dynamics during cell division."}],"keyword":["Cell Biology"],"author":[{"full_name":"Kutay, Ulrike","last_name":"Kutay","first_name":"Ulrike"},{"orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"date_updated":"2022-07-18T08:55:32Z","volume":20,"article_processing_charge":"No","_id":"11109","pmid":1,"extern":"1","publication_identifier":{"issn":["0955-0674"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa_version":"None","quality_controlled":"1","doi":"10.1016/j.ceb.2008.09.010","year":"2008","external_id":{"pmid":["18938243"]},"title":"Reorganization of the nuclear envelope during open mitosis","day":"01","type":"journal_article","intvolume":"        20","status":"public","issue":"6","publication":"Current Opinion in Cell Biology","page":"669-677","month":"12","article_type":"original","date_published":"2008-12-01T00:00:00Z","publisher":"Elsevier","scopus_import":"1","language":[{"iso":"eng"}],"date_created":"2022-04-07T07:55:00Z"},{"intvolume":"        18","status":"public","day":"01","type":"journal_article","publication":"Trends in Cell Biology","issue":"10","page":"456-466","scopus_import":"1","publisher":"Elsevier","language":[{"iso":"eng"}],"month":"10","date_published":"2008-10-01T00:00:00Z","article_type":"review","date_created":"2022-04-07T07:55:10Z","abstract":[{"lang":"eng","text":"Nuclear pore complexes are large aqueous channels that penetrate the nuclear envelope, thereby connecting the nuclear interior with the cytoplasm. Until recently, these macromolecular complexes were viewed as static structures, the only function of which was to control the molecular trafficking between the two compartments. It has now become evident that this simplistic scenario is inaccurate and that nuclear pore complexes are highly dynamic multiprotein assemblies involved in diverse cellular processes ranging from the organization of the cytoskeleton to gene expression. In this review, we discuss the most recent developments in the nuclear-pore-complex field, focusing on the assembly, disassembly, maintenance and function of this macromolecular structure."}],"keyword":["Cell Biology"],"author":[{"first_name":"Maximiliano A.","last_name":"D’Angelo","full_name":"D’Angelo, Maximiliano A."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"citation":{"chicago":"D’Angelo, Maximiliano A., and Martin Hetzer. “Structure, Dynamics and Function of Nuclear Pore Complexes.” <i>Trends in Cell Biology</i>. Elsevier, 2008. <a href=\"https://doi.org/10.1016/j.tcb.2008.07.009\">https://doi.org/10.1016/j.tcb.2008.07.009</a>.","apa":"D’Angelo, M. A., &#38; Hetzer, M. (2008). Structure, dynamics and function of nuclear pore complexes. <i>Trends in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.tcb.2008.07.009\">https://doi.org/10.1016/j.tcb.2008.07.009</a>","ieee":"M. A. D’Angelo and M. Hetzer, “Structure, dynamics and function of nuclear pore complexes,” <i>Trends in Cell Biology</i>, vol. 18, no. 10. Elsevier, pp. 456–466, 2008.","short":"M.A. D’Angelo, M. Hetzer, Trends in Cell Biology 18 (2008) 456–466.","ista":"D’Angelo MA, Hetzer M. 2008. Structure, dynamics and function of nuclear pore complexes. Trends in Cell Biology. 18(10), 456–466.","ama":"D’Angelo MA, Hetzer M. Structure, dynamics and function of nuclear pore complexes. <i>Trends in Cell Biology</i>. 2008;18(10):456-466. doi:<a href=\"https://doi.org/10.1016/j.tcb.2008.07.009\">10.1016/j.tcb.2008.07.009</a>","mla":"D’Angelo, Maximiliano A., and Martin Hetzer. “Structure, Dynamics and Function of Nuclear Pore Complexes.” <i>Trends in Cell Biology</i>, vol. 18, no. 10, Elsevier, 2008, pp. 456–66, doi:<a href=\"https://doi.org/10.1016/j.tcb.2008.07.009\">10.1016/j.tcb.2008.07.009</a>."},"publication_status":"published","extern":"1","publication_identifier":{"issn":["0962-8924"]},"_id":"11110","pmid":1,"oa_version":"None","quality_controlled":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","volume":18,"date_updated":"2022-07-18T08:55:33Z","title":"Structure, dynamics and function of nuclear pore complexes","external_id":{"pmid":["18786826"]},"doi":"10.1016/j.tcb.2008.07.009","year":"2008"},{"language":[{"iso":"eng"}],"publisher":"Rockefeller University Press","scopus_import":"1","date_published":"2008-09-08T00:00:00Z","article_type":"original","month":"09","date_created":"2022-04-07T07:55:23Z","status":"public","intvolume":"       182","type":"journal_article","day":"08","page":"911-924","issue":"5","publication":"Journal of Cell Biology","title":"Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation","external_id":{"pmid":["18779370"]},"doi":"10.1083/jcb.200805140","year":"2008","author":[{"first_name":"Daniel J.","full_name":"Anderson, Daniel J.","last_name":"Anderson"},{"first_name":"Martin W","last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"keyword":["Cell Biology"],"abstract":[{"lang":"eng","text":"During mitosis in metazoans, segregated chromosomes become enclosed by the nuclear envelope (NE), a double membrane that is continuous with the endoplasmic reticulum (ER). Recent in vitro data suggest that NE formation occurs by chromatin-mediated reorganization of the tubular ER; however, the basic principles of such a membrane-reshaping process remain uncharacterized. Here, we present a quantitative analysis of nuclear membrane assembly in mammalian cells using time-lapse microscopy. From the initial recruitment of ER tubules to chromatin, the formation of a membrane-enclosed, transport-competent nucleus occurs within ∼12 min. Overexpression of the ER tubule-forming proteins reticulon 3, reticulon 4, and DP1 inhibits NE formation and nuclear expansion, whereas their knockdown accelerates nuclear assembly. This suggests that the transition from membrane tubules to sheets is rate-limiting for nuclear assembly. Our results provide evidence that ER-shaping proteins are directly involved in the reconstruction of the nuclear compartment and that morphological restructuring of the ER is the principal mechanism of NE formation in vivo."}],"publication_status":"published","citation":{"ama":"Anderson DJ, Hetzer M. Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation. <i>Journal of Cell Biology</i>. 2008;182(5):911-924. doi:<a href=\"https://doi.org/10.1083/jcb.200805140\">10.1083/jcb.200805140</a>","mla":"Anderson, Daniel J., and Martin Hetzer. “Reshaping of the Endoplasmic Reticulum Limits the Rate for Nuclear Envelope Formation.” <i>Journal of Cell Biology</i>, vol. 182, no. 5, Rockefeller University Press, 2008, pp. 911–24, doi:<a href=\"https://doi.org/10.1083/jcb.200805140\">10.1083/jcb.200805140</a>.","short":"D.J. Anderson, M. Hetzer, Journal of Cell Biology 182 (2008) 911–924.","ista":"Anderson DJ, Hetzer M. 2008. Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation. Journal of Cell Biology. 182(5), 911–924.","ieee":"D. J. Anderson and M. Hetzer, “Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation,” <i>Journal of Cell Biology</i>, vol. 182, no. 5. Rockefeller University Press, pp. 911–924, 2008.","apa":"Anderson, D. J., &#38; Hetzer, M. (2008). Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.200805140\">https://doi.org/10.1083/jcb.200805140</a>","chicago":"Anderson, Daniel J., and Martin Hetzer. “Reshaping of the Endoplasmic Reticulum Limits the Rate for Nuclear Envelope Formation.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2008. <a href=\"https://doi.org/10.1083/jcb.200805140\">https://doi.org/10.1083/jcb.200805140</a>."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","quality_controlled":"1","oa_version":"None","_id":"11111","pmid":1,"extern":"1","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"volume":182,"date_updated":"2022-07-18T08:56:02Z","article_processing_charge":"No"},{"scopus_import":"1","publisher":"Elsevier","language":[{"iso":"eng"}],"month":"08","date_published":"2008-08-01T00:00:00Z","article_type":"original","date_created":"2022-04-07T07:55:34Z","intvolume":"        20","status":"public","day":"01","type":"journal_article","publication":"Current Opinion in Cell Biology","issue":"4","page":"386-392","external_id":{"pmid":["18495454"]},"title":"The life cycle of the metazoan nuclear envelope","year":"2008","doi":"10.1016/j.ceb.2008.03.016","abstract":[{"text":"The nuclear envelope is a double-layered membrane that encloses the nuclear genome and transcriptional machinery. In dividing cells of metazoa, the nucleus completely disassembles during mitosis, creating the need to re-establish the nuclear compartment at the end of each cell division. Given the crucial role of the nuclear envelope in gene regulation and cellular organization, it is not surprising that its biogenesis and organization have become active research areas. We will review recent insights into nuclear membrane dynamics during the cell cycle.","lang":"eng"}],"author":[{"last_name":"Anderson","full_name":"Anderson, Daniel J","first_name":"Daniel J"},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"keyword":["Cell Biology"],"citation":{"apa":"Anderson, D. J., &#38; Hetzer, M. (2008). The life cycle of the metazoan nuclear envelope. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2008.03.016\">https://doi.org/10.1016/j.ceb.2008.03.016</a>","ieee":"D. J. Anderson and M. Hetzer, “The life cycle of the metazoan nuclear envelope,” <i>Current Opinion in Cell Biology</i>, vol. 20, no. 4. Elsevier, pp. 386–392, 2008.","chicago":"Anderson, Daniel J, and Martin Hetzer. “The Life Cycle of the Metazoan Nuclear Envelope.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2008. <a href=\"https://doi.org/10.1016/j.ceb.2008.03.016\">https://doi.org/10.1016/j.ceb.2008.03.016</a>.","ama":"Anderson DJ, Hetzer M. The life cycle of the metazoan nuclear envelope. <i>Current Opinion in Cell Biology</i>. 2008;20(4):386-392. doi:<a href=\"https://doi.org/10.1016/j.ceb.2008.03.016\">10.1016/j.ceb.2008.03.016</a>","mla":"Anderson, Daniel J., and Martin Hetzer. “The Life Cycle of the Metazoan Nuclear Envelope.” <i>Current Opinion in Cell Biology</i>, vol. 20, no. 4, Elsevier, 2008, pp. 386–92, doi:<a href=\"https://doi.org/10.1016/j.ceb.2008.03.016\">10.1016/j.ceb.2008.03.016</a>.","ista":"Anderson DJ, Hetzer M. 2008. The life cycle of the metazoan nuclear envelope. Current Opinion in Cell Biology. 20(4), 386–392.","short":"D.J. Anderson, M. Hetzer, Current Opinion in Cell Biology 20 (2008) 386–392."},"publication_status":"published","publication_identifier":{"issn":["0955-0674"]},"extern":"1","pmid":1,"_id":"11112","oa_version":"None","quality_controlled":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","date_updated":"2022-07-18T08:56:07Z","volume":20},{"volume":121,"oa":1,"date_updated":"2022-07-18T08:56:10Z","article_processing_charge":"No","pmid":1,"_id":"11113","extern":"1","publication_identifier":{"eissn":["1477-9137"],"issn":["0021-9533"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","quality_controlled":"1","oa_version":"Published Version","publication_status":"published","citation":{"mla":"Anderson, Daniel J., and Martin Hetzer. “Shaping the Endoplasmic Reticulum into the Nuclear Envelope.” <i>Journal of Cell Science</i>, vol. 121, no. 2, The Company of Biologists, 2008, pp. 137–42, doi:<a href=\"https://doi.org/10.1242/jcs.005777\">10.1242/jcs.005777</a>.","ama":"Anderson DJ, Hetzer M. Shaping the endoplasmic reticulum into the nuclear envelope. <i>Journal of Cell Science</i>. 2008;121(2):137-142. doi:<a href=\"https://doi.org/10.1242/jcs.005777\">10.1242/jcs.005777</a>","short":"D.J. Anderson, M. Hetzer, Journal of Cell Science 121 (2008) 137–142.","ista":"Anderson DJ, Hetzer M. 2008. Shaping the endoplasmic reticulum into the nuclear envelope. Journal of Cell Science. 121(2), 137–142.","ieee":"D. J. Anderson and M. Hetzer, “Shaping the endoplasmic reticulum into the nuclear envelope,” <i>Journal of Cell Science</i>, vol. 121, no. 2. The Company of Biologists, pp. 137–142, 2008.","apa":"Anderson, D. J., &#38; Hetzer, M. (2008). Shaping the endoplasmic reticulum into the nuclear envelope. <i>Journal of Cell Science</i>. The Company of Biologists. <a href=\"https://doi.org/10.1242/jcs.005777\">https://doi.org/10.1242/jcs.005777</a>","chicago":"Anderson, Daniel J., and Martin Hetzer. “Shaping the Endoplasmic Reticulum into the Nuclear Envelope.” <i>Journal of Cell Science</i>. The Company of Biologists, 2008. <a href=\"https://doi.org/10.1242/jcs.005777\">https://doi.org/10.1242/jcs.005777</a>."},"abstract":[{"lang":"eng","text":"The nuclear envelope (NE), a double membrane enclosing the nucleus of eukaryotic cells, controls the flow of information between the nucleoplasm and the cytoplasm and provides a scaffold for the organization of chromatin and the cytoskeleton. In dividing metazoan cells, the NE breaks down at the onset of mitosis and then reforms around segregated chromosomes to generate the daughter nuclei. Recent data from intact cells and cell-free nuclear assembly systems suggest that the endoplasmic reticulum (ER) is the source of membrane for NE assembly. At the end of mitosis, ER membrane tubules are targeted to chromatin via tubule ends and reorganized into flat nuclear membrane sheets by specific DNA-binding membrane proteins. In contrast to previous models, which proposed vesicle fusion to be the principal mechanism of NE formation, these new studies suggest that the nuclear membrane forms by the chromatin-mediated reshaping of the ER."}],"keyword":["Cell Biology"],"author":[{"full_name":"Anderson, Daniel J.","last_name":"Anderson","first_name":"Daniel J."},{"first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1242/jcs.005777"}],"year":"2008","doi":"10.1242/jcs.005777","external_id":{"pmid":["18187447"]},"title":"Shaping the endoplasmic reticulum into the nuclear envelope","issue":"2","publication":"Journal of Cell Science","page":"137-142","day":"15","type":"journal_article","intvolume":"       121","status":"public","date_created":"2022-04-07T07:55:46Z","month":"01","date_published":"2008-01-15T00:00:00Z","article_type":"letter_note","publisher":"The Company of Biologists","scopus_import":"1","language":[{"iso":"eng"}]},{"article_processing_charge":"No","date_updated":"2022-07-18T08:56:38Z","volume":9,"oa_version":"None","quality_controlled":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication_identifier":{"issn":["1465-7392"],"eissn":["1476-4679"]},"extern":"1","_id":"11115","pmid":1,"citation":{"ieee":"D. J. Anderson and M. Hetzer, “Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum,” <i>Nature Cell Biology</i>, vol. 9, no. 10. Springer Nature, pp. 1160–1166, 2007.","apa":"Anderson, D. J., &#38; Hetzer, M. (2007). Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. <i>Nature Cell Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncb1636\">https://doi.org/10.1038/ncb1636</a>","chicago":"Anderson, Daniel J., and Martin Hetzer. “Nuclear Envelope Formation by Chromatin-Mediated Reorganization of the Endoplasmic Reticulum.” <i>Nature Cell Biology</i>. Springer Nature, 2007. <a href=\"https://doi.org/10.1038/ncb1636\">https://doi.org/10.1038/ncb1636</a>.","ama":"Anderson DJ, Hetzer M. Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. <i>Nature Cell Biology</i>. 2007;9(10):1160-1166. doi:<a href=\"https://doi.org/10.1038/ncb1636\">10.1038/ncb1636</a>","mla":"Anderson, Daniel J., and Martin Hetzer. “Nuclear Envelope Formation by Chromatin-Mediated Reorganization of the Endoplasmic Reticulum.” <i>Nature Cell Biology</i>, vol. 9, no. 10, Springer Nature, 2007, pp. 1160–66, doi:<a href=\"https://doi.org/10.1038/ncb1636\">10.1038/ncb1636</a>.","short":"D.J. Anderson, M. Hetzer, Nature Cell Biology 9 (2007) 1160–1166.","ista":"Anderson DJ, Hetzer M. 2007. Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nature Cell Biology. 9(10), 1160–1166."},"publication_status":"published","keyword":["Cell Biology"],"author":[{"full_name":"Anderson, Daniel J.","last_name":"Anderson","first_name":"Daniel J."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"}],"abstract":[{"text":"The formation of the nuclear envelope (NE) around chromatin is a major membrane-remodelling event that occurs during cell division of metazoa. It is unclear whether the nuclear membrane reforms by the fusion of NE fragments or if it re-emerges from an intact tubular network of the endoplasmic reticulum (ER). Here, we show that NE formation and expansion requires a tubular ER network and occurs efficiently in the presence of the membrane fusion inhibitor GTPγS. Chromatin recruitment of membranes, which is initiated by tubule-end binding, followed by the formation, expansion and sealing of flat membrane sheets, is mediated by DNA-binding proteins residing in the ER. Thus, chromatin plays an active role in reshaping of the ER during NE formation.","lang":"eng"}],"year":"2007","doi":"10.1038/ncb1636","title":"Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum","external_id":{"pmid":["17828249"]},"page":"1160-1166","publication":"Nature Cell Biology","issue":"10","type":"journal_article","day":"09","status":"public","intvolume":"         9","date_created":"2022-04-07T07:56:04Z","date_published":"2007-09-09T00:00:00Z","article_type":"original","month":"09","language":[{"iso":"eng"}],"scopus_import":"1","publisher":"Springer Nature"},{"oa_version":"None","quality_controlled":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","extern":"1","publication_identifier":{"eissn":["1420-9071"],"issn":["1420-682X"]},"pmid":1,"_id":"11117","article_processing_charge":"No","volume":63,"date_updated":"2022-07-18T08:56:58Z","author":[{"first_name":"M. A.","last_name":"D’Angelo","full_name":"D’Angelo, M. A."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W","first_name":"Martin W"}],"keyword":["Cell Biology","Cellular and Molecular Neuroscience","Pharmacology","Molecular Biology","Molecular Medicine"],"abstract":[{"lang":"eng","text":"Over the last years it has become evident that the nuclear envelope (NE) is more than a passive membrane barrier that separates the nucleus from the cytoplasm. The NE not only controls the trafficking of macromolecules between the nucleoplasm and the cytosol, but also provides anchoring sites for chromosomes and cytoskeleton to the nuclear periphery. Targeting of chromatin to the NE might actually be part of gene expression regulation in eukaryotes. Mutations in certain NE proteins are associated with a diversity of human diseases, including muscular dystrophy, neuropathy, lipodistrophy, torsion dystonia and the premature aging condition progeria. Despite the importance of the NE for cell division and differentiation, relatively little is known about its biogenesis and its role in human diseases. It is our goal to provide a comprehensive view of the NE and to discuss possible implications of NE-associated changes for gene expression, chromatin organization and signal transduction."}],"citation":{"ieee":"M. A. D’Angelo and M. Hetzer, “The role of the nuclear envelope in cellular organization,” <i>Cellular and Molecular Life Sciences</i>, vol. 63, no. 3. Springer Nature, pp. 316–332, 2006.","apa":"D’Angelo, M. A., &#38; Hetzer, M. (2006). The role of the nuclear envelope in cellular organization. <i>Cellular and Molecular Life Sciences</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s00018-005-5361-3\">https://doi.org/10.1007/s00018-005-5361-3</a>","chicago":"D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in Cellular Organization.” <i>Cellular and Molecular Life Sciences</i>. Springer Nature, 2006. <a href=\"https://doi.org/10.1007/s00018-005-5361-3\">https://doi.org/10.1007/s00018-005-5361-3</a>.","mla":"D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in Cellular Organization.” <i>Cellular and Molecular Life Sciences</i>, vol. 63, no. 3, Springer Nature, 2006, pp. 316–32, doi:<a href=\"https://doi.org/10.1007/s00018-005-5361-3\">10.1007/s00018-005-5361-3</a>.","ama":"D’Angelo MA, Hetzer M. The role of the nuclear envelope in cellular organization. <i>Cellular and Molecular Life Sciences</i>. 2006;63(3):316-332. doi:<a href=\"https://doi.org/10.1007/s00018-005-5361-3\">10.1007/s00018-005-5361-3</a>","short":"M.A. D’Angelo, M. Hetzer, Cellular and Molecular Life Sciences 63 (2006) 316–332.","ista":"D’Angelo MA, Hetzer M. 2006. The role of the nuclear envelope in cellular organization. Cellular and Molecular Life Sciences. 63(3), 316–332."},"publication_status":"published","title":"The role of the nuclear envelope in cellular organization","external_id":{"pmid":["16389459"]},"doi":"10.1007/s00018-005-5361-3","year":"2006","page":"316-332","publication":"Cellular and Molecular Life Sciences","issue":"3","status":"public","intvolume":"        63","type":"journal_article","day":"02","date_created":"2022-04-07T07:56:22Z","language":[{"iso":"eng"}],"scopus_import":"1","publisher":"Springer Nature","date_published":"2006-01-02T00:00:00Z","article_type":"review","month":"01"},{"type":"journal_article","day":"10","status":"public","intvolume":"        21","page":"347-380","publication":"Annual Review of Cell and Developmental Biology","article_type":"original","date_published":"2005-11-10T00:00:00Z","month":"11","language":[{"iso":"eng"}],"publisher":"Annual Reviews","scopus_import":"1","date_created":"2022-04-07T07:56:52Z","publication_status":"published","citation":{"chicago":"Hetzer, Martin, Tobias C. Walther, and Iain W. Mattaj. “Pushing the Envelope: Structure, Function, and Dynamics of the Nuclear Periphery.” <i>Annual Review of Cell and Developmental Biology</i>. Annual Reviews, 2005. <a href=\"https://doi.org/10.1146/annurev.cellbio.21.090704.151152\">https://doi.org/10.1146/annurev.cellbio.21.090704.151152</a>.","apa":"Hetzer, M., Walther, T. C., &#38; Mattaj, I. W. (2005). Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. <i>Annual Review of Cell and Developmental Biology</i>. Annual Reviews. <a href=\"https://doi.org/10.1146/annurev.cellbio.21.090704.151152\">https://doi.org/10.1146/annurev.cellbio.21.090704.151152</a>","ieee":"M. Hetzer, T. C. Walther, and I. W. Mattaj, “Pushing the envelope: Structure, function, and dynamics of the nuclear periphery,” <i>Annual Review of Cell and Developmental Biology</i>, vol. 21. Annual Reviews, pp. 347–380, 2005.","ista":"Hetzer M, Walther TC, Mattaj IW. 2005. Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. Annual Review of Cell and Developmental Biology. 21, 347–380.","short":"M. Hetzer, T.C. Walther, I.W. Mattaj, Annual Review of Cell and Developmental Biology 21 (2005) 347–380.","ama":"Hetzer M, Walther TC, Mattaj IW. Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. <i>Annual Review of Cell and Developmental Biology</i>. 2005;21:347-380. doi:<a href=\"https://doi.org/10.1146/annurev.cellbio.21.090704.151152\">10.1146/annurev.cellbio.21.090704.151152</a>","mla":"Hetzer, Martin, et al. “Pushing the Envelope: Structure, Function, and Dynamics of the Nuclear Periphery.” <i>Annual Review of Cell and Developmental Biology</i>, vol. 21, Annual Reviews, 2005, pp. 347–80, doi:<a href=\"https://doi.org/10.1146/annurev.cellbio.21.090704.151152\">10.1146/annurev.cellbio.21.090704.151152</a>."},"keyword":["Cell Biology","Developmental Biology"],"author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W","first_name":"Martin W"},{"first_name":"Tobias C.","last_name":"Walther","full_name":"Walther, Tobias C."},{"full_name":"Mattaj, Iain W.","last_name":"Mattaj","first_name":"Iain W."}],"abstract":[{"lang":"eng","text":"The nuclear envelope (NE) is a highly specialized membrane that delineates the eukaryotic cell nucleus. It is composed of the inner and outer nuclear membranes, nuclear pore complexes (NPCs) and, in metazoa, the lamina. The NE not only regulates the trafficking of macromolecules between nucleoplasm and cytosol but also provides anchoring sites for chromatin and the cytoskeleton. Through these interactions, the NE helps position the nucleus within the cell and chromosomes within the nucleus, thereby regulating the expression of certain genes. The NE is not static, rather it is continuously remodeled during cell division. The most dramatic example of NE reorganization occurs during mitosis in metazoa when the NE undergoes a complete cycle of disassembly and reformation. Despite the importance of the NE for eukaryotic cell life, relatively little is known about its biogenesis or many of its functions. We thus are far from understanding the molecular etiology of a diverse group of NE-associated diseases."}],"volume":21,"date_updated":"2022-07-18T08:57:34Z","article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa_version":"None","quality_controlled":"1","pmid":1,"_id":"11120","publication_identifier":{"eissn":["1530-8995"],"issn":["1081-0706"]},"extern":"1","doi":"10.1146/annurev.cellbio.21.090704.151152","year":"2005","external_id":{"pmid":["16212499"]},"title":"Pushing the envelope: Structure, function, and dynamics of the nuclear periphery"},{"citation":{"chicago":"Hetzer, Martin, Oliver J. Gruss, and Iain W. Mattaj. “The Ran GTPase as a Marker of Chromosome Position in Spindle Formation and Nuclear Envelope Assembly.” <i>Nature Cell Biology</i>. Springer Nature, 2002. <a href=\"https://doi.org/10.1038/ncb0702-e177\">https://doi.org/10.1038/ncb0702-e177</a>.","apa":"Hetzer, M., Gruss, O. J., &#38; Mattaj, I. W. (2002). The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. <i>Nature Cell Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncb0702-e177\">https://doi.org/10.1038/ncb0702-e177</a>","ieee":"M. Hetzer, O. J. Gruss, and I. W. Mattaj, “The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly,” <i>Nature Cell Biology</i>, vol. 4, no. 7. Springer Nature, pp. E177–E184, 2002.","short":"M. Hetzer, O.J. Gruss, I.W. Mattaj, Nature Cell Biology 4 (2002) E177–E184.","ista":"Hetzer M, Gruss OJ, Mattaj IW. 2002. The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. Nature Cell Biology. 4(7), E177–E184.","ama":"Hetzer M, Gruss OJ, Mattaj IW. The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. <i>Nature Cell Biology</i>. 2002;4(7):E177-E184. doi:<a href=\"https://doi.org/10.1038/ncb0702-e177\">10.1038/ncb0702-e177</a>","mla":"Hetzer, Martin, et al. “The Ran GTPase as a Marker of Chromosome Position in Spindle Formation and Nuclear Envelope Assembly.” <i>Nature Cell Biology</i>, vol. 4, no. 7, Springer Nature, 2002, pp. E177–84, doi:<a href=\"https://doi.org/10.1038/ncb0702-e177\">10.1038/ncb0702-e177</a>."},"publication_status":"published","abstract":[{"lang":"eng","text":"The small GTPase Ran is a key regulator of nucleocytoplasmic transport during interphase. The asymmetric distribution of the GTP-bound form of Ran across the nuclear envelope — that is, large quantities in the nucleus compared with small quantities in the cytoplasm — determines the directionality of many nuclear transport processes. Recent findings that Ran also functions in spindle formation and nuclear envelope assembly during mitosis suggest that Ran has a general role in chromatin-centred processes. Ran functions in these events as a signal for chromosome position."}],"author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W"},{"first_name":"Oliver J.","full_name":"Gruss, Oliver J.","last_name":"Gruss"},{"full_name":"Mattaj, Iain W.","last_name":"Mattaj","first_name":"Iain W."}],"keyword":["Cell Biology"],"article_processing_charge":"No","date_updated":"2022-07-18T08:58:03Z","volume":4,"extern":"1","publication_identifier":{"issn":["1465-7392"],"eissn":["1476-4679"]},"_id":"11123","pmid":1,"oa_version":"None","quality_controlled":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","doi":"10.1038/ncb0702-e177","year":"2002","external_id":{"pmid":["12105431"]},"title":"The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly","day":"01","type":"journal_article","intvolume":"         4","status":"public","publication":"Nature Cell Biology","issue":"7","page":"E177-E184","month":"07","date_published":"2002-07-01T00:00:00Z","article_type":"original","scopus_import":"1","publisher":"Springer Nature","language":[{"iso":"eng"}],"date_created":"2022-04-07T07:57:19Z"},{"_id":"13438","pmid":1,"publication_identifier":{"issn":["0021-9258"]},"extern":"1","acknowledgement":"We are grateful to D. E. Clapham, E. Wöll, G. Meyer, and G. Botta for helpful discussion and/or reading of the manuscript. We also thank T. Stiernagle for providing the N2 strain of C. elegans and A. Wimmer and M. Frick for technical assistance","user_id":"ea97e931-d5af-11eb-85d4-e6957dddbf17","oa_version":"Published Version","quality_controlled":"1","oa":1,"volume":277,"date_updated":"2023-08-01T12:55:54Z","article_processing_charge":"No","abstract":[{"text":"ICln is an ion channel identified by expression cloning using a cDNA library from Madin-Darby canine kidney cells. In all organisms tested so far, only one transcript for the ICln protein could be identified. Here we show that two splice variants of the ICln ion channel can be found in Caenorhabditis elegans. Moreover, we show that these two splice variants of the ICln channel protein, which we termed IClnN1 and IClnN2, can be functionally reconstituted and tested in an artificial lipid bilayer. In these experiments, the IClnN1-induced currents showed no voltage-dependent inactivation, whereas the IClnN2-induced currents fully inactivated at positive potentials. The molecular entity responsible for the voltage-dependent inactivation of IClnN2 is a cluster of positively charged amino acids encoded by exon 2a, which is absent in IClnN1. Our experiments suggest a mechanism of channel inactivation that is similar to the “ball and chain” model proposed for the Shaker potassium channel,i.e. a cluster of positively charged amino acids hinders ion permeation through the channel by a molecular and voltage-dependent interaction at the inner vestibulum of the pore. This hypothesis is supported by the finding that synthetic peptides with the same amino acid sequence as the positive cluster can transform the IClnN1-induced current to the current observed after reconstitution of IClnN2. Furthermore, we show that the nematode ICln gene is embedded in an operon harboring two additional genes, which we termed Nx and Ny. Co-reconstitution of Nx and IClnN2 and functional analysis of the related currents revealed a functional interaction between the two proteins, as evidenced by the fact that the IClnN2-induced current in the presence of Nx was no longer voltage-sensitive. The experiments described indicate that the genome organization in nematodes allows an effective approach for the identification of functional partner proteins of ion channels.","lang":"eng"}],"keyword":["Cell Biology","Molecular Biology","Biochemistry"],"author":[{"first_name":"Johannes","full_name":"Fürst, Johannes","last_name":"Fürst"},{"first_name":"Markus","full_name":"Ritter, Markus","last_name":"Ritter"},{"first_name":"Jakob","full_name":"Rudzki, Jakob","last_name":"Rudzki"},{"id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87","first_name":"Johann G","orcid":"0000-0001-8559-3973","full_name":"Danzl, Johann G","last_name":"Danzl"},{"first_name":"Martin","full_name":"Gschwentner, Martin","last_name":"Gschwentner"},{"full_name":"Scandella, Elke","last_name":"Scandella","first_name":"Elke"},{"first_name":"Martin","last_name":"Jakab","full_name":"Jakab, Martin"},{"full_name":"König, Matthias","last_name":"König","first_name":"Matthias"},{"first_name":"Bernhard","last_name":"Oehl","full_name":"Oehl, Bernhard"},{"first_name":"Florian","full_name":"Lang, Florian","last_name":"Lang"},{"last_name":"Deetjen","full_name":"Deetjen, Peter","first_name":"Peter"},{"first_name":"Markus","last_name":"Paulmichl","full_name":"Paulmichl, Markus"}],"publication_status":"published","citation":{"chicago":"Fürst, Johannes, Markus Ritter, Jakob Rudzki, Johann G Danzl, Martin Gschwentner, Elke Scandella, Martin Jakab, et al. “ICln Ion Channel Splice Variants in Caenorhabditis Elegans.” <i>Journal of Biological Chemistry</i>. Elsevier, 2002. <a href=\"https://doi.org/10.1074/jbc.m107372200\">https://doi.org/10.1074/jbc.m107372200</a>.","apa":"Fürst, J., Ritter, M., Rudzki, J., Danzl, J. G., Gschwentner, M., Scandella, E., … Paulmichl, M. (2002). ICln Ion channel splice variants in Caenorhabditis elegans. <i>Journal of Biological Chemistry</i>. Elsevier. <a href=\"https://doi.org/10.1074/jbc.m107372200\">https://doi.org/10.1074/jbc.m107372200</a>","ieee":"J. Fürst <i>et al.</i>, “ICln Ion channel splice variants in Caenorhabditis elegans,” <i>Journal of Biological Chemistry</i>, vol. 277, no. 6. Elsevier, pp. 4435–4445, 2002.","ista":"Fürst J, Ritter M, Rudzki J, Danzl JG, Gschwentner M, Scandella E, Jakab M, König M, Oehl B, Lang F, Deetjen P, Paulmichl M. 2002. ICln Ion channel splice variants in Caenorhabditis elegans. Journal of Biological Chemistry. 277(6), 4435–4445.","short":"J. Fürst, M. Ritter, J. Rudzki, J.G. Danzl, M. Gschwentner, E. Scandella, M. Jakab, M. König, B. Oehl, F. Lang, P. Deetjen, M. Paulmichl, Journal of Biological Chemistry 277 (2002) 4435–4445.","ama":"Fürst J, Ritter M, Rudzki J, et al. ICln Ion channel splice variants in Caenorhabditis elegans. <i>Journal of Biological Chemistry</i>. 2002;277(6):4435-4445. doi:<a href=\"https://doi.org/10.1074/jbc.m107372200\">10.1074/jbc.m107372200</a>","mla":"Fürst, Johannes, et al. “ICln Ion Channel Splice Variants in Caenorhabditis Elegans.” <i>Journal of Biological Chemistry</i>, vol. 277, no. 6, Elsevier, 2002, pp. 4435–45, doi:<a href=\"https://doi.org/10.1074/jbc.m107372200\">10.1074/jbc.m107372200</a>."},"ddc":["570"],"tmp":{"image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"title":"ICln Ion channel splice variants in Caenorhabditis elegans","external_id":{"pmid":["11706026"]},"year":"2002","doi":"10.1074/jbc.m107372200","issue":"6","publication":"Journal of Biological Chemistry","page":"4435-4445","file_date_updated":"2023-08-01T12:44:09Z","intvolume":"       277","status":"public","day":"08","type":"journal_article","date_created":"2023-08-01T12:37:50Z","file":[{"access_level":"open_access","date_updated":"2023-08-01T12:44:09Z","checksum":"13abe20f78eb37ab62beb006f62c69b7","date_created":"2023-08-01T12:44:09Z","file_size":798920,"file_name":"2002_JBC_Fuerst.pdf","file_id":"13439","creator":"alisjak","relation":"main_file","content_type":"application/pdf","success":1}],"license":"https://creativecommons.org/licenses/by/4.0/","has_accepted_license":"1","publisher":"Elsevier","scopus_import":"1","language":[{"iso":"eng"}],"month":"02","article_type":"original","date_published":"2002-02-08T00:00:00Z"}]