[{"oa_version":"Published Version","month":"02","publication":"Aging","language":[{"iso":"eng"}],"keyword":["Cell Biology","Aging"],"publication_identifier":{"issn":["1945-4589"]},"oa":1,"date_published":"2010-02-01T00:00:00Z","type":"journal_article","main_file_link":[{"url":"https://doi.org/10.18632/aging.100125","open_access":"1"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:52:58Z","title":"The role of the nuclear pore complex in aging of post-mitotic cells","intvolume":"         2","pmid":1,"_id":"11098","scopus_import":"1","author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W"}],"issue":"2","publisher":"Impact Journals","article_type":"original","page":"74-75","quality_controlled":"1","doi":"10.18632/aging.100125","day":"01","date_updated":"2022-07-18T08:54:15Z","year":"2010","citation":{"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>","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>","ista":"Hetzer M. 2010. The role of the nuclear pore complex in aging of post-mitotic cells. Aging. 2(2), 74–75.","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>.","short":"M. Hetzer, Aging 2 (2010) 74–75."},"external_id":{"pmid":["20354266"]},"volume":2,"extern":"1"},{"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."}],"doi":"10.1074/jbc.m109.061168","day":"19","publication_identifier":{"issn":["0021-9258","1083-351X"]},"date_published":"2010-02-19T00:00:00Z","type":"journal_article","date_updated":"2021-01-12T08:19:31Z","citation":{"ista":"Corazza A, Rennella E, Schanda P, Mimmi MC, Cutuil T, Raimondi S, Giorgetti S, Fogolari F, Viglino P, Frydman L, Gal M, Bellotti V, Brutscher B, Esposito G. 2010. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. Journal of Biological Chemistry. 285(8), 5827–5835.","short":"A. Corazza, E. Rennella, P. Schanda, M.C. Mimmi, T. Cutuil, S. Raimondi, S. Giorgetti, F. Fogolari, P. Viglino, L. Frydman, M. Gal, V. Bellotti, B. Brutscher, G. Esposito, Journal of Biological Chemistry 285 (2010) 5827–5835.","mla":"Corazza, Alessandra, et al. “Native-Unlike Long-Lived Intermediates along the Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin Revealed by Real-Time Two-Dimensional NMR.” <i>Journal of Biological Chemistry</i>, vol. 285, no. 8, American Society for Biochemistry &#38; Molecular Biology, 2010, pp. 5827–35, doi:<a href=\"https://doi.org/10.1074/jbc.m109.061168\">10.1074/jbc.m109.061168</a>.","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.","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>.","ama":"Corazza A, Rennella E, Schanda P, et al. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. <i>Journal of Biological Chemistry</i>. 2010;285(8):5827-5835. doi:<a href=\"https://doi.org/10.1074/jbc.m109.061168\">10.1074/jbc.m109.061168</a>","apa":"Corazza, A., Rennella, E., Schanda, P., Mimmi, M. C., Cutuil, T., Raimondi, S., … Esposito, G. (2010). Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology. <a href=\"https://doi.org/10.1074/jbc.m109.061168\">https://doi.org/10.1074/jbc.m109.061168</a>"},"year":"2010","extern":"1","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","volume":285,"month":"02","title":"Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR","intvolume":"       285","oa_version":"None","publication_status":"published","article_processing_charge":"No","date_created":"2020-09-18T10:11:23Z","author":[{"full_name":"Corazza, Alessandra","first_name":"Alessandra","last_name":"Corazza"},{"last_name":"Rennella","first_name":"Enrico","full_name":"Rennella, Enrico"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda"},{"last_name":"Mimmi","first_name":"Maria Chiara","full_name":"Mimmi, Maria Chiara"},{"full_name":"Cutuil, Thomas","last_name":"Cutuil","first_name":"Thomas"},{"first_name":"Sara","last_name":"Raimondi","full_name":"Raimondi, Sara"},{"full_name":"Giorgetti, Sofia","last_name":"Giorgetti","first_name":"Sofia"},{"full_name":"Fogolari, Federico","first_name":"Federico","last_name":"Fogolari"},{"last_name":"Viglino","first_name":"Paolo","full_name":"Viglino, Paolo"},{"full_name":"Frydman, Lucio","last_name":"Frydman","first_name":"Lucio"},{"full_name":"Gal, Maayan","first_name":"Maayan","last_name":"Gal"},{"full_name":"Bellotti, Vittorio","first_name":"Vittorio","last_name":"Bellotti"},{"full_name":"Brutscher, Bernhard","last_name":"Brutscher","first_name":"Bernhard"},{"last_name":"Esposito","first_name":"Gennaro","full_name":"Esposito, Gennaro"}],"issue":"8","_id":"8473","publication":"Journal of Biological Chemistry","article_type":"original","publisher":"American Society for Biochemistry & Molecular Biology","language":[{"iso":"eng"}],"keyword":["Cell Biology","Biochemistry","Molecular Biology"],"page":"5827-5835","quality_controlled":"1"},{"publication_identifier":{"issn":["1477-9129","0950-1991"]},"date_published":"2010-07-15T00:00:00Z","type":"journal_article","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"None","month":"07","publication":"Development","language":[{"iso":"eng"}],"keyword":["Developmental Biology","Molecular Biology","Anther Tapetum","Arabidopsis","Cell Fate Establishment","EMS1","Reproductive Cell Lineage"],"doi":"10.1242/dev.049320","day":"15","abstract":[{"text":"The four microsporangia of the flowering plant anther develop from archesporial cells in the L2 of the primordium. Within each microsporangium, developing microsporocytes are surrounded by concentric monolayers of tapetal, middle layer and endothecial cells. How this intricate array of tissues, each containing relatively few cells, is established in an organ possessing no formal meristems is poorly understood. We describe here the pivotal role of the LRR receptor kinase EXCESS MICROSPOROCYTES 1 (EMS1) in forming the monolayer of tapetal nurse cells in Arabidopsis. Unusually for plants, tapetal cells are specified very early in development, and are subsequently stimulated to proliferate by a receptor-like kinase (RLK) complex that includes EMS1. Mutations in members of this EMS1 signalling complex and its putative ligand result in male-sterile plants in which tapetal initials fail to proliferate. Surprisingly, these cells continue to develop, isolated at the locular periphery. Mutant and wild-type microsporangia expand at similar rates and the ‘tapetal’ space at the periphery of mutant locules becomes occupied by microsporocytes. However, induction of late expression of EMS1 in the few tapetal initials in ems1 plants results in their proliferation to generate a functional tapetum, and this proliferation suppresses microsporocyte number. Our experiments also show that integrity of the tapetal monolayer is crucial for the maintenance of the polarity of divisions within it. This unexpected autonomy of the tapetal ‘lineage’ is discussed in the context of tissue development in complex plant organs, where constancy in size, shape and cell number is crucial.","lang":"eng"}],"date_updated":"2023-05-08T10:57:11Z","citation":{"ama":"Feng X, Dickinson HG. Tapetal cell fate, lineage and proliferation in the Arabidopsis anther. <i>Development</i>. 2010;137(14):2409-2416. doi:<a href=\"https://doi.org/10.1242/dev.049320\">10.1242/dev.049320</a>","apa":"Feng, X., &#38; Dickinson, H. G. (2010). Tapetal cell fate, lineage and proliferation in the Arabidopsis anther. <i>Development</i>. The Company of Biologists. <a href=\"https://doi.org/10.1242/dev.049320\">https://doi.org/10.1242/dev.049320</a>","chicago":"Feng, Xiaoqi, and Hugh G. Dickinson. “Tapetal Cell Fate, Lineage and Proliferation in the Arabidopsis Anther.” <i>Development</i>. The Company of Biologists, 2010. <a href=\"https://doi.org/10.1242/dev.049320\">https://doi.org/10.1242/dev.049320</a>.","ieee":"X. Feng and H. G. Dickinson, “Tapetal cell fate, lineage and proliferation in the Arabidopsis anther,” <i>Development</i>, vol. 137, no. 14. The Company of Biologists, pp. 2409–2416, 2010.","short":"X. Feng, H.G. Dickinson, Development 137 (2010) 2409–2416.","mla":"Feng, Xiaoqi, and Hugh G. Dickinson. “Tapetal Cell Fate, Lineage and Proliferation in the Arabidopsis Anther.” <i>Development</i>, vol. 137, no. 14, The Company of Biologists, 2010, pp. 2409–16, doi:<a href=\"https://doi.org/10.1242/dev.049320\">10.1242/dev.049320</a>.","ista":"Feng X, Dickinson HG. 2010. Tapetal cell fate, lineage and proliferation in the Arabidopsis anther. Development. 137(14), 2409–2416."},"year":"2010","external_id":{"pmid":["20570940"]},"volume":137,"acknowledgement":"We thank the following for providing mutant lines and reagents: Hong Ma, De Ye, Sacco De Vries, and Rod Scott for providing the pA9::Barnase lines and information on A9 expression patterns. Carla Galinha and Paolo Piazza gave valuable help with in situ hybridisation and qRT-PCR, respectively, and we acknowledge Qing Zhang, Helen Prescott and Matthew Dicks for providing excellent technical assistance. We are indebted to Miltos Tsiantis and Angela Hay for helpful discussion, and the research was funded by Oxford University through a Clarendon Scholarship to X.F., with additional financial support from Magdalen College (Oxford).","extern":"1","publication_status":"published","article_processing_charge":"No","department":[{"_id":"XiFe"}],"date_created":"2023-01-16T09:21:54Z","title":"Tapetal cell fate, lineage and proliferation in the Arabidopsis anther","intvolume":"       137","_id":"12199","pmid":1,"scopus_import":"1","author":[{"orcid":"0000-0002-4008-1234","full_name":"Feng, Xiaoqi","first_name":"Xiaoqi","last_name":"Feng","id":"e0164712-22ee-11ed-b12a-d80fcdf35958"},{"full_name":"Dickinson, Hugh G.","last_name":"Dickinson","first_name":"Hugh G."}],"issue":"14","publisher":"The Company of Biologists","article_type":"original","page":"2409-2416","quality_controlled":"1"},{"department":[{"_id":"XiFe"}],"date_created":"2023-01-16T09:22:18Z","article_processing_charge":"No","publication_status":"published","intvolume":"        38","title":"Cell–cell interactions during patterning of the <i>Arabidopsis</i> anther","scopus_import":"1","pmid":1,"_id":"12200","issue":"2","author":[{"first_name":"Xiaoqi","last_name":"Feng","orcid":"0000-0002-4008-1234","full_name":"Feng, Xiaoqi","id":"e0164712-22ee-11ed-b12a-d80fcdf35958"},{"last_name":"Dickinson","first_name":"Hugh G.","full_name":"Dickinson, Hugh G."}],"publisher":"Portland Press Ltd.","article_type":"original","quality_controlled":"1","page":"571-576","day":"22","doi":"10.1042/bst0380571","abstract":[{"text":"Key steps in the evolution of the angiosperm anther include the patterning of the concentrically organized microsporangium and the incorporation of four such microsporangia into a leaf-like structure. Mutant studies in the model plant Arabidopsis thaliana are leading to an increasingly accurate picture of (i) the cell lineages culminating in the different cell types present in the microsporangium (the microsporocytes, the tapetum, and the middle and endothecial layers), and (ii) some of the genes responsible for specifying their fates. However, the processes that confer polarity on the developing anther and position the microsporangia within it remain unclear. Certainly, data from a range of experimental strategies suggest that hormones play a central role in establishing polarity and the patterning of the anther initial, and may be responsible for locating the microsporangia. But the fact that microsporangia were originally positioned externally suggests that their development is likely to be autonomous, perhaps with the reproductive cells generating signals controlling the growth and division of the investing anther epidermis. These possibilities are discussed in the context of the expression of genes which initiate and maintain male and female reproductive development, and in the perspective of our current views of anther evolution.","lang":"eng"}],"citation":{"chicago":"Feng, Xiaoqi, and Hugh G. Dickinson. “Cell–Cell Interactions during Patterning of the <i>Arabidopsis</i> Anther.” <i>Biochemical Society Transactions</i>. Portland Press Ltd., 2010. <a href=\"https://doi.org/10.1042/bst0380571\">https://doi.org/10.1042/bst0380571</a>.","ieee":"X. Feng and H. G. Dickinson, “Cell–cell interactions during patterning of the <i>Arabidopsis</i> anther,” <i>Biochemical Society Transactions</i>, vol. 38, no. 2. Portland Press Ltd., pp. 571–576, 2010.","apa":"Feng, X., &#38; Dickinson, H. G. (2010). Cell–cell interactions during patterning of the <i>Arabidopsis</i> anther. <i>Biochemical Society Transactions</i>. Portland Press Ltd. <a href=\"https://doi.org/10.1042/bst0380571\">https://doi.org/10.1042/bst0380571</a>","ama":"Feng X, Dickinson HG. Cell–cell interactions during patterning of the <i>Arabidopsis</i> anther. <i>Biochemical Society Transactions</i>. 2010;38(2):571-576. doi:<a href=\"https://doi.org/10.1042/bst0380571\">10.1042/bst0380571</a>","ista":"Feng X, Dickinson HG. 2010. Cell–cell interactions during patterning of the <i>Arabidopsis</i> anther. Biochemical Society Transactions. 38(2), 571–576.","short":"X. Feng, H.G. Dickinson, Biochemical Society Transactions 38 (2010) 571–576.","mla":"Feng, Xiaoqi, and Hugh G. Dickinson. “Cell–Cell Interactions during Patterning of the <i>Arabidopsis</i> Anther.” <i>Biochemical Society Transactions</i>, vol. 38, no. 2, Portland Press Ltd., 2010, pp. 571–76, doi:<a href=\"https://doi.org/10.1042/bst0380571\">10.1042/bst0380571</a>."},"year":"2010","date_updated":"2023-05-08T10:57:59Z","external_id":{"pmid":["20298223"]},"volume":38,"extern":"1","oa_version":"None","month":"03","publication":"Biochemical Society Transactions","keyword":["Biochemistry","Anther Development","Arabidopsis","Cell Fate","Microsporangium","Polarity","Receptor Kinase"],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["0300-5127","1470-8752"]},"type":"journal_article","date_published":"2010-03-22T00:00:00Z","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87"},{"external_id":{"pmid":["19922866"]},"date_updated":"2022-07-18T08:55:01Z","citation":{"apa":"Hetzer, M., &#38; Wente, S. R. (2009). Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. <i>Developmental Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">https://doi.org/10.1016/j.devcel.2009.10.007</a>","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>","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>.","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>.","short":"M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.","ista":"Hetzer M, Wente SR. 2009. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. Developmental Cell. 17(5), 606–616."},"year":"2009","abstract":[{"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."}],"doi":"10.1016/j.devcel.2009.10.007","day":"17","extern":"1","volume":17,"author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"},{"full_name":"Wente, Susan R.","first_name":"Susan R.","last_name":"Wente"}],"issue":"5","pmid":1,"_id":"11103","scopus_import":"1","title":"Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes","intvolume":"        17","publication_status":"published","date_created":"2022-04-07T07:53:45Z","article_processing_charge":"No","page":"606-616","quality_controlled":"1","article_type":"review","publisher":"Elsevier","date_published":"2009-11-17T00:00:00Z","type":"journal_article","oa":1,"publication_identifier":{"issn":["1534-5807"]},"status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2009.10.007"}],"publication":"Developmental Cell","month":"11","oa_version":"Published Version","language":[{"iso":"eng"}],"keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"]},{"oa":1,"publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"date_published":"2009-07-20T00:00:00Z","type":"journal_article","related_material":{"link":[{"url":"https://doi.org/10.1083/jcb.20090110620090903c","relation":"erratum"}]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","main_file_link":[{"url":"https://doi.org/10.1083/jcb.200901106","open_access":"1"}],"month":"07","oa_version":"Published Version","publication":"Journal of Cell Biology","language":[{"iso":"eng"}],"keyword":["Cell Biology"],"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"}],"doi":"10.1083/jcb.200901106","day":"20","external_id":{"pmid":["19620630"]},"date_updated":"2022-07-18T08:58:35Z","year":"2009","citation":{"short":"D.J. Anderson, J.D. Vargas, J.P. Hsiao, M. Hetzer, Journal of Cell Biology 186 (2009) 183–191.","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>.","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.","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>","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>","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.","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>."},"extern":"1","volume":186,"title":"Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo","intvolume":"       186","publication_status":"published","date_created":"2022-04-07T07:54:18Z","article_processing_charge":"No","author":[{"last_name":"Anderson","first_name":"Daniel J.","full_name":"Anderson, Daniel J."},{"first_name":"Jesse D.","last_name":"Vargas","full_name":"Vargas, Jesse D."},{"first_name":"Joshua P.","last_name":"Hsiao","full_name":"Hsiao, Joshua P."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"issue":"2","_id":"11106","pmid":1,"scopus_import":"1","article_type":"original","publisher":"Rockefeller University Press","page":"183-191","quality_controlled":"1"},{"language":[{"iso":"eng"}],"keyword":["Cell Biology"],"oa_version":"Published Version","month":"03","publication":"Journal of Cell Biology","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.200806174"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"oa":1,"date_published":"2009-03-09T00:00:00Z","type":"journal_article","publisher":"Rockefeller University Press","article_type":"original","page":"659-675","quality_controlled":"1","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:54:44Z","title":"ER membrane–bending proteins are necessary for de novo nuclear pore formation","intvolume":"       184","pmid":1,"_id":"11107","scopus_import":"1","author":[{"first_name":"T. Renee","last_name":"Dawson","full_name":"Dawson, T. Renee"},{"first_name":"Michelle D.","last_name":"Lazarus","full_name":"Lazarus, Michelle D."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"},{"full_name":"Wente, Susan R.","first_name":"Susan R.","last_name":"Wente"}],"issue":"5","volume":184,"extern":"1","doi":"10.1083/jcb.200806174","day":"09","abstract":[{"lang":"eng","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."}],"date_updated":"2022-07-18T08:55:05Z","year":"2009","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>","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>","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>.","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.","short":"T.R. Dawson, M.D. Lazarus, M. Hetzer, S.R. Wente, Journal of Cell Biology 184 (2009) 659–675.","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>.","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."},"external_id":{"pmid":["19273614"]}},{"oa_version":"None","month":"12","publication":"Current Opinion in Cell Biology","keyword":["Cell Biology"],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["0955-0674"]},"type":"journal_article","date_published":"2008-12-01T00:00:00Z","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","date_created":"2022-04-07T07:55:00Z","publication_status":"published","intvolume":"        20","title":"Reorganization of the nuclear envelope during open mitosis","scopus_import":"1","_id":"11109","pmid":1,"issue":"6","author":[{"full_name":"Kutay, Ulrike","first_name":"Ulrike","last_name":"Kutay"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W"}],"publisher":"Elsevier","article_type":"original","quality_controlled":"1","page":"669-677","day":"01","doi":"10.1016/j.ceb.2008.09.010","abstract":[{"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.","lang":"eng"}],"year":"2008","citation":{"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>","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>","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.","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>.","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>.","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."},"date_updated":"2022-07-18T08:55:32Z","external_id":{"pmid":["18938243"]},"volume":20,"extern":"1"},{"extern":"1","volume":18,"abstract":[{"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.","lang":"eng"}],"doi":"10.1016/j.tcb.2008.07.009","day":"01","external_id":{"pmid":["18786826"]},"date_updated":"2022-07-18T08:55:33Z","year":"2008","citation":{"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.","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>.","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>","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>","ista":"D’Angelo MA, Hetzer M. 2008. Structure, dynamics and function of nuclear pore complexes. Trends in Cell Biology. 18(10), 456–466.","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>.","short":"M.A. D’Angelo, M. Hetzer, Trends in Cell Biology 18 (2008) 456–466."},"article_type":"review","publisher":"Elsevier","page":"456-466","quality_controlled":"1","title":"Structure, dynamics and function of nuclear pore complexes","intvolume":"        18","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:55:10Z","author":[{"first_name":"Maximiliano A.","last_name":"D’Angelo","full_name":"D’Angelo, Maximiliano A."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"issue":"10","_id":"11110","pmid":1,"scopus_import":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","publication_identifier":{"issn":["0962-8924"]},"date_published":"2008-10-01T00:00:00Z","type":"journal_article","language":[{"iso":"eng"}],"keyword":["Cell Biology"],"month":"10","oa_version":"None","publication":"Trends in Cell Biology"},{"status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","type":"journal_article","date_published":"2008-09-08T00:00:00Z","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"keyword":["Cell Biology"],"language":[{"iso":"eng"}],"publication":"Journal of Cell Biology","oa_version":"None","month":"09","volume":182,"extern":"1","citation":{"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>.","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>","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>","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.","short":"D.J. Anderson, M. Hetzer, Journal of Cell Biology 182 (2008) 911–924.","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>."},"year":"2008","date_updated":"2022-07-18T08:56:02Z","external_id":{"pmid":["18779370"]},"day":"08","doi":"10.1083/jcb.200805140","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."}],"quality_controlled":"1","page":"911-924","publisher":"Rockefeller University Press","article_type":"original","scopus_import":"1","_id":"11111","pmid":1,"issue":"5","author":[{"last_name":"Anderson","first_name":"Daniel J.","full_name":"Anderson, Daniel J."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"date_created":"2022-04-07T07:55:23Z","article_processing_charge":"No","publication_status":"published","intvolume":"       182","title":"Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation"},{"keyword":["Cell Biology"],"language":[{"iso":"eng"}],"oa_version":"None","month":"08","publication":"Current Opinion in Cell Biology","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication_identifier":{"issn":["0955-0674"]},"type":"journal_article","date_published":"2008-08-01T00:00:00Z","publisher":"Elsevier","article_type":"original","quality_controlled":"1","page":"386-392","date_created":"2022-04-07T07:55:34Z","article_processing_charge":"No","publication_status":"published","intvolume":"        20","title":"The life cycle of the metazoan nuclear envelope","scopus_import":"1","pmid":1,"_id":"11112","issue":"4","author":[{"full_name":"Anderson, Daniel J","last_name":"Anderson","first_name":"Daniel J"},{"first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"volume":20,"extern":"1","day":"01","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"}],"year":"2008","citation":{"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>","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>","ista":"Anderson DJ, Hetzer M. 2008. The life cycle of the metazoan nuclear envelope. Current Opinion in Cell Biology. 20(4), 386–392.","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>.","short":"D.J. Anderson, M. Hetzer, Current Opinion in Cell Biology 20 (2008) 386–392."},"date_updated":"2022-07-18T08:56:07Z","external_id":{"pmid":["18495454"]}},{"abstract":[{"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.","lang":"eng"}],"doi":"10.1242/jcs.005777","day":"15","external_id":{"pmid":["18187447"]},"date_updated":"2022-07-18T08:56:10Z","year":"2008","citation":{"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.","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>.","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>","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>","ista":"Anderson DJ, Hetzer M. 2008. Shaping the endoplasmic reticulum into the nuclear envelope. Journal of Cell Science. 121(2), 137–142.","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>.","short":"D.J. Anderson, M. Hetzer, Journal of Cell Science 121 (2008) 137–142."},"extern":"1","volume":121,"title":"Shaping the endoplasmic reticulum into the nuclear envelope","intvolume":"       121","publication_status":"published","date_created":"2022-04-07T07:55:46Z","article_processing_charge":"No","author":[{"full_name":"Anderson, Daniel J.","last_name":"Anderson","first_name":"Daniel J."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"issue":"2","_id":"11113","pmid":1,"scopus_import":"1","article_type":"letter_note","publisher":"The Company of Biologists","page":"137-142","quality_controlled":"1","oa":1,"publication_identifier":{"eissn":["1477-9137"],"issn":["0021-9533"]},"date_published":"2008-01-15T00:00:00Z","type":"journal_article","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1242/jcs.005777"}],"month":"01","oa_version":"Published Version","publication":"Journal of Cell Science","language":[{"iso":"eng"}],"keyword":["Cell Biology"]},{"oa_version":"None","month":"09","publication":"Nature Cell Biology","language":[{"iso":"eng"}],"keyword":["Cell Biology"],"publication_identifier":{"eissn":["1476-4679"],"issn":["1465-7392"]},"date_published":"2007-09-09T00:00:00Z","type":"journal_article","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:56:04Z","title":"Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum","intvolume":"         9","pmid":1,"_id":"11115","scopus_import":"1","author":[{"last_name":"Anderson","first_name":"Daniel J.","full_name":"Anderson, Daniel J."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"issue":"10","publisher":"Springer Nature","article_type":"original","page":"1160-1166","quality_controlled":"1","doi":"10.1038/ncb1636","day":"09","abstract":[{"lang":"eng","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."}],"date_updated":"2022-07-18T08:56:38Z","citation":{"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>.","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>","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>","ista":"Anderson DJ, Hetzer M. 2007. Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nature Cell Biology. 9(10), 1160–1166.","short":"D.J. Anderson, M. Hetzer, Nature Cell Biology 9 (2007) 1160–1166.","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>."},"year":"2007","external_id":{"pmid":["17828249"]},"volume":9,"extern":"1"},{"publication_identifier":{"eissn":["1420-9071"],"issn":["1420-682X"]},"date_published":"2006-01-02T00:00:00Z","type":"journal_article","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","oa_version":"None","month":"01","publication":"Cellular and Molecular Life Sciences","language":[{"iso":"eng"}],"keyword":["Cell Biology","Cellular and Molecular Neuroscience","Pharmacology","Molecular Biology","Molecular Medicine"],"doi":"10.1007/s00018-005-5361-3","day":"02","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."}],"date_updated":"2022-07-18T08:56:58Z","year":"2006","citation":{"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>.","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.","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>","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>","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.","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>.","short":"M.A. D’Angelo, M. Hetzer, Cellular and Molecular Life Sciences 63 (2006) 316–332."},"external_id":{"pmid":["16389459"]},"volume":63,"extern":"1","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:56:22Z","title":"The role of the nuclear envelope in cellular organization","intvolume":"        63","pmid":1,"_id":"11117","scopus_import":"1","author":[{"full_name":"D’Angelo, M. A.","first_name":"M. A.","last_name":"D’Angelo"},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"issue":"3","publisher":"Springer Nature","article_type":"review","page":"316-332","quality_controlled":"1"},{"volume":21,"extern":"1","day":"10","doi":"10.1146/annurev.cellbio.21.090704.151152","abstract":[{"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.","lang":"eng"}],"year":"2005","citation":{"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>","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>","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>.","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.","short":"M. Hetzer, T.C. Walther, I.W. Mattaj, Annual Review of Cell and Developmental Biology 21 (2005) 347–380.","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>.","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."},"date_updated":"2022-07-18T08:57:34Z","external_id":{"pmid":["16212499"]},"publisher":"Annual Reviews","article_type":"original","quality_controlled":"1","page":"347-380","article_processing_charge":"No","date_created":"2022-04-07T07:56:52Z","publication_status":"published","intvolume":"        21","title":"Pushing the envelope: Structure, function, and dynamics of the nuclear periphery","scopus_import":"1","pmid":1,"_id":"11120","author":[{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"full_name":"Walther, Tobias C.","first_name":"Tobias C.","last_name":"Walther"},{"first_name":"Iain W.","last_name":"Mattaj","full_name":"Mattaj, Iain W."}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","publication_identifier":{"eissn":["1530-8995"],"issn":["1081-0706"]},"type":"journal_article","date_published":"2005-11-10T00:00:00Z","keyword":["Cell Biology","Developmental Biology"],"language":[{"iso":"eng"}],"oa_version":"None","month":"11","publication":"Annual Review of Cell and Developmental Biology"},{"publication":"Nature Cell Biology","month":"07","oa_version":"None","language":[{"iso":"eng"}],"keyword":["Cell Biology"],"date_published":"2002-07-01T00:00:00Z","type":"journal_article","publication_identifier":{"eissn":["1476-4679"],"issn":["1465-7392"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","author":[{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"full_name":"Gruss, Oliver J.","last_name":"Gruss","first_name":"Oliver J."},{"full_name":"Mattaj, Iain W.","first_name":"Iain W.","last_name":"Mattaj"}],"issue":"7","_id":"11123","pmid":1,"scopus_import":"1","title":"The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly","intvolume":"         4","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:57:19Z","page":"E177-E184","quality_controlled":"1","article_type":"original","publisher":"Springer Nature","external_id":{"pmid":["12105431"]},"date_updated":"2022-07-18T08:58:03Z","citation":{"short":"M. Hetzer, O.J. Gruss, I.W. Mattaj, Nature Cell Biology 4 (2002) E177–E184.","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>.","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.","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>","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>","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>.","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."},"year":"2002","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."}],"doi":"10.1038/ncb0702-e177","day":"01","extern":"1","volume":4},{"external_id":{"pmid":["11706026"]},"date_updated":"2023-08-01T12:55:54Z","citation":{"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.","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>.","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>","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>","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.","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>."},"year":"2002","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"}],"doi":"10.1074/jbc.m107372200","day":"08","extern":"1","ddc":["570"],"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","volume":277,"author":[{"full_name":"Fürst, Johannes","first_name":"Johannes","last_name":"Fürst"},{"first_name":"Markus","last_name":"Ritter","full_name":"Ritter, Markus"},{"full_name":"Rudzki, Jakob","first_name":"Jakob","last_name":"Rudzki"},{"id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-8559-3973","full_name":"Danzl, Johann G","first_name":"Johann G","last_name":"Danzl"},{"full_name":"Gschwentner, Martin","first_name":"Martin","last_name":"Gschwentner"},{"last_name":"Scandella","first_name":"Elke","full_name":"Scandella, Elke"},{"last_name":"Jakab","first_name":"Martin","full_name":"Jakab, Martin"},{"first_name":"Matthias","last_name":"König","full_name":"König, Matthias"},{"full_name":"Oehl, Bernhard","first_name":"Bernhard","last_name":"Oehl"},{"full_name":"Lang, Florian","last_name":"Lang","first_name":"Florian"},{"full_name":"Deetjen, Peter","first_name":"Peter","last_name":"Deetjen"},{"last_name":"Paulmichl","first_name":"Markus","full_name":"Paulmichl, Markus"}],"issue":"6","_id":"13438","pmid":1,"scopus_import":"1","license":"https://creativecommons.org/licenses/by/4.0/","title":"ICln Ion channel splice variants in Caenorhabditis elegans","intvolume":"       277","publication_status":"published","article_processing_charge":"No","date_created":"2023-08-01T12:37:50Z","file_date_updated":"2023-08-01T12:44:09Z","page":"4435-4445","quality_controlled":"1","article_type":"original","publisher":"Elsevier","date_published":"2002-02-08T00:00:00Z","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"oa":1,"publication_identifier":{"issn":["0021-9258"]},"user_id":"ea97e931-d5af-11eb-85d4-e6957dddbf17","status":"public","file":[{"date_created":"2023-08-01T12:44:09Z","file_size":798920,"checksum":"13abe20f78eb37ab62beb006f62c69b7","date_updated":"2023-08-01T12:44:09Z","file_name":"2002_JBC_Fuerst.pdf","content_type":"application/pdf","relation":"main_file","success":1,"access_level":"open_access","file_id":"13439","creator":"alisjak"}],"publication":"Journal of Biological Chemistry","has_accepted_license":"1","month":"02","oa_version":"Published Version","language":[{"iso":"eng"}],"keyword":["Cell Biology","Molecular Biology","Biochemistry"]},{"quality_controlled":"1","page":"1086-1091","publisher":"Springer Nature","article_type":"original","scopus_import":"1","pmid":1,"_id":"11125","issue":"12","author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"},{"last_name":"Meyer","first_name":"Hemmo H.","full_name":"Meyer, Hemmo H."},{"full_name":"Walther, Tobias C.","first_name":"Tobias C.","last_name":"Walther"},{"last_name":"Bilbao-Cortes","first_name":"Daniel","full_name":"Bilbao-Cortes, Daniel"},{"full_name":"Warren, Graham","first_name":"Graham","last_name":"Warren"},{"first_name":"Iain W.","last_name":"Mattaj","full_name":"Mattaj, Iain W."}],"article_processing_charge":"No","date_created":"2022-04-07T07:57:42Z","publication_status":"published","intvolume":"         3","title":"Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly","volume":3,"extern":"1","citation":{"short":"M. Hetzer, H.H. Meyer, T.C. Walther, D. Bilbao-Cortes, G. Warren, I.W. Mattaj, Nature Cell Biology 3 (2001) 1086–1091.","mla":"Hetzer, Martin, et al. “Distinct AAA-ATPase P97 Complexes Function in Discrete Steps of Nuclear Assembly.” <i>Nature Cell Biology</i>, vol. 3, no. 12, Springer Nature, 2001, pp. 1086–91, doi:<a href=\"https://doi.org/10.1038/ncb1201-1086\">10.1038/ncb1201-1086</a>.","ista":"Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. 2001. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nature Cell Biology. 3(12), 1086–1091.","ama":"Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. <i>Nature Cell Biology</i>. 2001;3(12):1086-1091. doi:<a href=\"https://doi.org/10.1038/ncb1201-1086\">10.1038/ncb1201-1086</a>","apa":"Hetzer, M., Meyer, H. H., Walther, T. C., Bilbao-Cortes, D., Warren, G., &#38; Mattaj, I. W. (2001). Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. <i>Nature Cell Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncb1201-1086\">https://doi.org/10.1038/ncb1201-1086</a>","ieee":"M. Hetzer, H. H. Meyer, T. C. Walther, D. Bilbao-Cortes, G. Warren, and I. W. Mattaj, “Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly,” <i>Nature Cell Biology</i>, vol. 3, no. 12. Springer Nature, pp. 1086–1091, 2001.","chicago":"Hetzer, Martin, Hemmo H. Meyer, Tobias C. Walther, Daniel Bilbao-Cortes, Graham Warren, and Iain W. Mattaj. “Distinct AAA-ATPase P97 Complexes Function in Discrete Steps of Nuclear Assembly.” <i>Nature Cell Biology</i>. Springer Nature, 2001. <a href=\"https://doi.org/10.1038/ncb1201-1086\">https://doi.org/10.1038/ncb1201-1086</a>."},"year":"2001","date_updated":"2022-07-18T08:58:07Z","external_id":{"pmid":["11781570"]},"day":"02","doi":"10.1038/ncb1201-1086","abstract":[{"text":"Although nuclear envelope (NE) assembly is known to require the GTPase Ran, the membrane fusion machinery involved is uncharacterized. NE assembly involves formation of a reticular network on chromatin, fusion of this network into a closed NE and subsequent expansion. Here we show that p97, an AAA-ATPase previously implicated in fusion of Golgi and transitional endoplasmic reticulum (ER) membranes together with the adaptor p47, has two discrete functions in NE assembly. Formation of a closed NE requires the p97–Ufd1–Npl4 complex, not previously implicated in membrane fusion. Subsequent NE growth involves a p97–p47 complex. This study provides the first insights into the molecular mechanisms and specificity of fusion events involved in NE formation.","lang":"eng"}],"keyword":["Cell Biology"],"language":[{"iso":"eng"}],"publication":"Nature Cell Biology","oa_version":"None","month":"11","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","type":"journal_article","date_published":"2001-11-02T00:00:00Z","publication_identifier":{"issn":["1465-7392"],"eissn":["1476-4679"]}},{"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","type":"journal_article","date_published":"2000-01-24T00:00:00Z","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"keyword":["Cell Biology"],"language":[{"iso":"eng"}],"publication":"Journal of Cell Biology","oa_version":"None","month":"01","volume":148,"extern":"1","year":"2000","citation":{"mla":"Hetzer, Martin, and Iain W. Mattaj. “An Atp-Dependent, Ran-Independent Mechanism for Nuclear Import of the U1a and U2b′′ Spliceosome Proteins.” <i>Journal of Cell Biology</i>, vol. 148, no. 2, Rockefeller University Press, 2000, pp. 293–304, doi:<a href=\"https://doi.org/10.1083/jcb.148.2.293\">10.1083/jcb.148.2.293</a>.","short":"M. Hetzer, I.W. Mattaj, Journal of Cell Biology 148 (2000) 293–304.","ista":"Hetzer M, Mattaj IW. 2000. An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins. Journal of Cell Biology. 148(2), 293–304.","apa":"Hetzer, M., &#38; Mattaj, I. W. (2000). An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.148.2.293\">https://doi.org/10.1083/jcb.148.2.293</a>","ama":"Hetzer M, Mattaj IW. An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins. <i>Journal of Cell Biology</i>. 2000;148(2):293-304. doi:<a href=\"https://doi.org/10.1083/jcb.148.2.293\">10.1083/jcb.148.2.293</a>","ieee":"M. Hetzer and I. W. Mattaj, “An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins,” <i>Journal of Cell Biology</i>, vol. 148, no. 2. Rockefeller University Press, pp. 293–304, 2000.","chicago":"Hetzer, Martin, and Iain W. Mattaj. “An Atp-Dependent, Ran-Independent Mechanism for Nuclear Import of the U1a and U2b′′ Spliceosome Proteins.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2000. <a href=\"https://doi.org/10.1083/jcb.148.2.293\">https://doi.org/10.1083/jcb.148.2.293</a>."},"date_updated":"2022-07-18T08:58:29Z","external_id":{"pmid":["10648562"]},"day":"24","doi":"10.1083/jcb.148.2.293","abstract":[{"text":"Nuclear import of the two uracil-rich small nuclear ribonucleoprotein (U snRNP) components U1A and U2B′′ is mediated by unusually long and complex nuclear localization signals (NLSs). Here we investigate nuclear import of U1A and U2B′′ in vitro and demonstrate that it occurs by an active, saturable process. Several lines of evidence suggest that import of the two proteins occurs by an import mechanism different to those characterized previously. No cross competition is seen with a variety of previously studied NLSs. In contrast to import mediated by members of the importin-β family of nucleocytoplasmic transport receptors, U1A/U2B′′ import is not inhibited by either nonhydrolyzable guanosine triphosphate (GTP) analogues or by a mutant of the GTPase Ran that is incapable of GTP hydrolysis. Adenosine triphosphate is capable of supporting U1A and U2B′′ import, whereas neither nonhydrolyzable adenosine triphosphate analogues nor GTP can do so. U1A and U2B′′ import in vitro does not require the addition of soluble cytosolic proteins, but a factor or factors required for U1A and U2B′′ import remains tightly associated with the nuclear fraction of conventionally permeabilized cells. This activity can be solubilized in the presence of elevated MgCl2. These data suggest that U1A and U2B′′ import into the nucleus occurs by a hitherto uncharacterized mechanism.","lang":"eng"}],"quality_controlled":"1","page":"293-304","publisher":"Rockefeller University Press","article_type":"original","scopus_import":"1","_id":"11126","pmid":1,"issue":"2","author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"},{"last_name":"Mattaj","first_name":"Iain W.","full_name":"Mattaj, Iain W."}],"date_created":"2022-04-07T07:57:49Z","article_processing_charge":"No","publication_status":"published","intvolume":"       148","title":"An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins"},{"intvolume":"         5","title":"GTP hydrolysis by Ran is required for nuclear envelope assembly","date_created":"2022-04-07T07:57:59Z","article_processing_charge":"No","publication_status":"published","issue":"6","author":[{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"last_name":"Bilbao-Cortés","first_name":"Daniel","full_name":"Bilbao-Cortés, Daniel"},{"full_name":"Walther, Tobias C","first_name":"Tobias C","last_name":"Walther"},{"last_name":"Gruss","first_name":"Oliver J","full_name":"Gruss, Oliver J"},{"last_name":"Mattaj","first_name":"Iain W","full_name":"Mattaj, Iain W"}],"scopus_import":"1","_id":"11127","pmid":1,"article_type":"original","publisher":"Elsevier","quality_controlled":"1","page":"1013-1024","abstract":[{"text":"Nuclear formation in Xenopus egg extracts requires cytosol and is inhibited by GTPγS, indicating a requirement for GTPase activity. Nuclear envelope (NE) vesicle fusion is extensively inhibited by GTPγS and two mutant forms of the Ran GTPase, Q69L and T24N. Depletion of either Ran or RCC1, the exchange factor for Ran, from the assembly reaction also inhibits this step of NE formation. Ran depletion can be complemented by the addition of Ran loaded with either GTP or GDP but not with GTPγS. RCC1 depletion is only complemented by RCC1 itself or by RanGTP. Thus, generation of RanGTP by RCC1 and GTP hydrolysis by Ran are both required for the extensive membrane fusion events that lead to NE formation.","lang":"eng"}],"day":"01","doi":"10.1016/s1097-2765(00)80266-x","external_id":{"pmid":["10911995"]},"citation":{"short":"M. Hetzer, D. Bilbao-Cortés, T.C. Walther, O.J. Gruss, I.W. Mattaj, Molecular Cell 5 (2000) 1013–1024.","mla":"Hetzer, Martin, et al. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.” <i>Molecular Cell</i>, vol. 5, no. 6, Elsevier, 2000, pp. 1013–24, doi:<a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">10.1016/s1097-2765(00)80266-x</a>.","ista":"Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. 2000. GTP hydrolysis by Ran is required for nuclear envelope assembly. Molecular Cell. 5(6), 1013–1024.","ama":"Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. GTP hydrolysis by Ran is required for nuclear envelope assembly. <i>Molecular Cell</i>. 2000;5(6):1013-1024. doi:<a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">10.1016/s1097-2765(00)80266-x</a>","apa":"Hetzer, M., Bilbao-Cortés, D., Walther, T. C., Gruss, O. J., &#38; Mattaj, I. W. (2000). GTP hydrolysis by Ran is required for nuclear envelope assembly. <i>Molecular Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">https://doi.org/10.1016/s1097-2765(00)80266-x</a>","ieee":"M. Hetzer, D. Bilbao-Cortés, T. C. Walther, O. J. Gruss, and I. W. Mattaj, “GTP hydrolysis by Ran is required for nuclear envelope assembly,” <i>Molecular Cell</i>, vol. 5, no. 6. Elsevier, pp. 1013–1024, 2000.","chicago":"Hetzer, Martin, Daniel Bilbao-Cortés, Tobias C Walther, Oliver J Gruss, and Iain W Mattaj. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.” <i>Molecular Cell</i>. Elsevier, 2000. <a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">https://doi.org/10.1016/s1097-2765(00)80266-x</a>."},"year":"2000","date_updated":"2022-07-18T08:58:31Z","extern":"1","volume":5,"month":"06","oa_version":"Published Version","publication":"Molecular Cell","keyword":["Cell Biology","Molecular Biology"],"language":[{"iso":"eng"}],"oa":1,"publication_identifier":{"issn":["1097-2765"]},"type":"journal_article","date_published":"2000-06-01T00:00:00Z","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/S1097-2765(00)80266-X"}]}]