[{"oa_version":"None","month":"04","publication":"Cold Spring Harbor Symposia on Quantitative Biology","keyword":["Genetics","Molecular Biology","Biochemistry"],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["0091-7451","1943-4456"],"isbn":["9781936113071"]},"type":"journal_article","date_published":"2011-04-18T00:00:00Z","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","date_created":"2022-04-07T07:53:18Z","publication_status":"published","intvolume":"        75","title":"Nuclear pore complexes: Guardians of the nuclear genome","scopus_import":"1","_id":"11100","pmid":1,"author":[{"full_name":"Capelson, M.","last_name":"Capelson","first_name":"M."},{"last_name":"Doucet","first_name":"C.","full_name":"Doucet, C."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W"}],"publisher":"Cold Spring Harbor Laboratory Press","article_type":"original","quality_controlled":"1","page":"585-597","day":"18","doi":"10.1101/sqb.2010.75.059","abstract":[{"lang":"eng","text":"Eukaryotic cell function depends on the physical separation of nucleoplasmic and cytoplasmic components by the nuclear envelope (NE). Molecular communication between the two compartments involves active, signal-mediated trafficking, a function that is exclusively performed by nuclear pore complexes (NPCs). The individual NPC components and the mechanisms that are involved in nuclear trafficking are well documented and have become textbook knowledge. However, in addition to their roles as nuclear gatekeepers, NPC components-nucleoporins-have been shown to have critical roles in chromatin organization and gene regulation. These findings have sparked new enthusiasm to study the roles of this multiprotein complex in nuclear organization and explore novel functions that in some cases appear to go beyond a role in transport. Here, we discuss our present view of NPC biogenesis, which is tightly linked to proper cell cycle progression and cell differentiation. In addition, we summarize new data suggesting that NPCs represent dynamic hubs for the integration of gene regulation and nuclear transport processes."}],"year":"2011","citation":{"mla":"Capelson, M., et al. “Nuclear Pore Complexes: Guardians of the Nuclear Genome.” <i>Cold Spring Harbor Symposia on Quantitative Biology</i>, vol. 75, Cold Spring Harbor Laboratory Press, 2011, pp. 585–97, doi:<a href=\"https://doi.org/10.1101/sqb.2010.75.059\">10.1101/sqb.2010.75.059</a>.","short":"M. Capelson, C. Doucet, M. Hetzer, Cold Spring Harbor Symposia on Quantitative Biology 75 (2011) 585–597.","ista":"Capelson M, Doucet C, Hetzer M. 2011. Nuclear pore complexes: Guardians of the nuclear genome. Cold Spring Harbor Symposia on Quantitative Biology. 75, 585–597.","apa":"Capelson, M., Doucet, C., &#38; Hetzer, M. (2011). Nuclear pore complexes: Guardians of the nuclear genome. <i>Cold Spring Harbor Symposia on Quantitative Biology</i>. Cold Spring Harbor Laboratory Press. <a href=\"https://doi.org/10.1101/sqb.2010.75.059\">https://doi.org/10.1101/sqb.2010.75.059</a>","ama":"Capelson M, Doucet C, Hetzer M. Nuclear pore complexes: Guardians of the nuclear genome. <i>Cold Spring Harbor Symposia on Quantitative Biology</i>. 2011;75:585-597. doi:<a href=\"https://doi.org/10.1101/sqb.2010.75.059\">10.1101/sqb.2010.75.059</a>","ieee":"M. Capelson, C. Doucet, and M. Hetzer, “Nuclear pore complexes: Guardians of the nuclear genome,” <i>Cold Spring Harbor Symposia on Quantitative Biology</i>, vol. 75. Cold Spring Harbor Laboratory Press, pp. 585–597, 2011.","chicago":"Capelson, M., C. Doucet, and Martin Hetzer. “Nuclear Pore Complexes: Guardians of the Nuclear Genome.” <i>Cold Spring Harbor Symposia on Quantitative Biology</i>. Cold Spring Harbor Laboratory Press, 2011. <a href=\"https://doi.org/10.1101/sqb.2010.75.059\">https://doi.org/10.1101/sqb.2010.75.059</a>."},"date_updated":"2022-07-18T08:54:23Z","external_id":{"pmid":["21502404"]},"volume":75,"extern":"1"},{"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","volume":12,"type":"journal_article","date_published":"2011-02-15T00:00:00Z","year":"2011","citation":{"apa":"Huber, M., Hiller, S., Schanda, P., Ernst, M., Böckmann, A., Verel, R., &#38; Meier, B. H. (2011). A proton-detected 4D solid-state NMR experiment for protein structure determination. <i>ChemPhysChem</i>. Wiley. <a href=\"https://doi.org/10.1002/cphc.201100062\">https://doi.org/10.1002/cphc.201100062</a>","ama":"Huber M, Hiller S, Schanda P, et al. A proton-detected 4D solid-state NMR experiment for protein structure determination. <i>ChemPhysChem</i>. 2011;12(5):915-918. doi:<a href=\"https://doi.org/10.1002/cphc.201100062\">10.1002/cphc.201100062</a>","ieee":"M. Huber <i>et al.</i>, “A proton-detected 4D solid-state NMR experiment for protein structure determination,” <i>ChemPhysChem</i>, vol. 12, no. 5. Wiley, pp. 915–918, 2011.","chicago":"Huber, Matthias, Sebastian Hiller, Paul Schanda, Matthias Ernst, Anja Böckmann, René Verel, and Beat H. Meier. “A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.” <i>ChemPhysChem</i>. Wiley, 2011. <a href=\"https://doi.org/10.1002/cphc.201100062\">https://doi.org/10.1002/cphc.201100062</a>.","mla":"Huber, Matthias, et al. “A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.” <i>ChemPhysChem</i>, vol. 12, no. 5, Wiley, 2011, pp. 915–18, doi:<a href=\"https://doi.org/10.1002/cphc.201100062\">10.1002/cphc.201100062</a>.","short":"M. Huber, S. Hiller, P. Schanda, M. Ernst, A. Böckmann, R. Verel, B.H. Meier, ChemPhysChem 12 (2011) 915–918.","ista":"Huber M, Hiller S, Schanda P, Ernst M, Böckmann A, Verel R, Meier BH. 2011. A proton-detected 4D solid-state NMR experiment for protein structure determination. ChemPhysChem. 12(5), 915–918."},"date_updated":"2021-01-12T08:19:30Z","abstract":[{"lang":"eng","text":"Adding a new dimension: 4D or 3D proton‐detected spectra of perdeuterated protein samples with 1H labelled amides and methyl groups permit collecting unambiguous distance restraints with high sensitivity and determining protein structure by solid‐state NMR (see picture)."}],"day":"15","publication_identifier":{"issn":["1439-4235"]},"doi":"10.1002/cphc.201100062","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"language":[{"iso":"eng"}],"quality_controlled":"1","page":"915-918","article_type":"original","publisher":"Wiley","issue":"5","author":[{"last_name":"Huber","first_name":"Matthias","full_name":"Huber, Matthias"},{"last_name":"Hiller","first_name":"Sebastian","full_name":"Hiller, Sebastian"},{"orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"full_name":"Ernst, Matthias","first_name":"Matthias","last_name":"Ernst"},{"first_name":"Anja","last_name":"Böckmann","full_name":"Böckmann, Anja"},{"full_name":"Verel, René","last_name":"Verel","first_name":"René"},{"last_name":"Meier","first_name":"Beat H.","full_name":"Meier, Beat H."}],"_id":"8470","publication":"ChemPhysChem","intvolume":"        12","month":"02","title":"A proton-detected 4D solid-state NMR experiment for protein structure determination","date_created":"2020-09-18T10:10:56Z","article_processing_charge":"No","oa_version":"None","publication_status":"published"},{"publication_identifier":{"issn":["1943-0264"]},"date_published":"2010-02-03T00:00:00Z","type":"journal_article","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa_version":"None","month":"02","publication":"Cold Spring Harbor Perspectives in Biology","language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"doi":"10.1101/cshperspect.a000539","day":"03","abstract":[{"text":"The nuclear envelope (NE) is a highly regulated membrane barrier that separates the nucleus from the cytoplasm in eukaryotic cells. It contains a large number of different proteins that have been implicated in chromatin organization and gene regulation. Although the nuclear membrane enables complex levels of gene expression, it also poses a challenge when it comes to cell division. To allow access of the mitotic spindle to chromatin, the nucleus of metazoans must completely disassemble during mitosis, generating the need to re-establish the nuclear compartment at the end of each cell division. Here, I summarize our current understanding of the dynamic remodeling of the NE during the cell cycle.","lang":"eng"}],"date_updated":"2022-07-18T08:53:50Z","citation":{"ista":"Hetzer M. 2010. The nuclear envelope. Cold Spring Harbor Perspectives in Biology. 2(3), a000539–a000539.","short":"M. Hetzer, Cold Spring Harbor Perspectives in Biology 2 (2010) a000539–a000539.","mla":"Hetzer, Martin. “The Nuclear Envelope.” <i>Cold Spring Harbor Perspectives in Biology</i>, vol. 2, no. 3, Cold Spring Harbor Laboratory, 2010, pp. a000539–a000539, doi:<a href=\"https://doi.org/10.1101/cshperspect.a000539\">10.1101/cshperspect.a000539</a>.","chicago":"Hetzer, Martin. “The Nuclear Envelope.” <i>Cold Spring Harbor Perspectives in Biology</i>. Cold Spring Harbor Laboratory, 2010. <a href=\"https://doi.org/10.1101/cshperspect.a000539\">https://doi.org/10.1101/cshperspect.a000539</a>.","ieee":"M. Hetzer, “The nuclear envelope,” <i>Cold Spring Harbor Perspectives in Biology</i>, vol. 2, no. 3. Cold Spring Harbor Laboratory, pp. a000539–a000539, 2010.","ama":"Hetzer M. The nuclear envelope. <i>Cold Spring Harbor Perspectives in Biology</i>. 2010;2(3):a000539-a000539. doi:<a href=\"https://doi.org/10.1101/cshperspect.a000539\">10.1101/cshperspect.a000539</a>","apa":"Hetzer, M. (2010). The nuclear envelope. <i>Cold Spring Harbor Perspectives in Biology</i>. Cold Spring Harbor Laboratory. <a href=\"https://doi.org/10.1101/cshperspect.a000539\">https://doi.org/10.1101/cshperspect.a000539</a>"},"year":"2010","external_id":{"pmid":["20300205"]},"volume":2,"extern":"1","publication_status":"published","date_created":"2022-04-07T07:52:49Z","article_processing_charge":"No","title":"The nuclear envelope","intvolume":"         2","_id":"11097","pmid":1,"scopus_import":"1","author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"issue":"3","publisher":"Cold Spring Harbor Laboratory","article_type":"original","page":"a000539-a000539","quality_controlled":"1"},{"article_type":"original","publisher":"Elsevier","page":"1030-1041","quality_controlled":"1","title":"Cell cycle-dependent differences in nuclear pore complex assembly in metazoa","intvolume":"       141","publication_status":"published","date_created":"2022-04-07T07:53:29Z","article_processing_charge":"No","author":[{"first_name":"Christine M.","last_name":"Doucet","full_name":"Doucet, Christine M."},{"full_name":"Talamas, Jessica A.","first_name":"Jessica A.","last_name":"Talamas"},{"first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"issue":"6","pmid":1,"_id":"11101","scopus_import":"1","extern":"1","volume":141,"abstract":[{"lang":"eng","text":"In metazoa, nuclear pore complexes (NPCs) assemble from disassembled precursors into a reforming nuclear envelope (NE) at the end of mitosis and into growing intact NEs during interphase. Here, we show via RNAi-mediated knockdown that ELYS, a nucleoporin critical for the recruitment of the essential Nup107/160 complex to chromatin, is required for NPC assembly at the end of mitosis but not during interphase. Conversely, the transmembrane nucleoporin POM121 is critical for the incorporation of the Nup107/160 complex into new assembly sites specifically during interphase. Strikingly, recruitment of the Nup107/160 complex to an intact NE involves a membrane curvature-sensing domain of its constituent Nup133, which is not required for postmitotic NPC formation. Our results suggest that in organisms with open mitosis, NPCs assemble via two distinct mechanisms to accommodate cell cycle-dependent differences in NE topology."}],"doi":"10.1016/j.cell.2010.04.036","day":"11","external_id":{"pmid":["20550937"]},"date_updated":"2022-07-18T08:54:52Z","citation":{"ista":"Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041.","short":"C.M. Doucet, J.A. Talamas, M. Hetzer, Cell 141 (2010) 1030–1041.","mla":"Doucet, Christine M., et al. “Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa.” <i>Cell</i>, vol. 141, no. 6, Elsevier, 2010, pp. 1030–41, doi:<a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">10.1016/j.cell.2010.04.036</a>.","chicago":"Doucet, Christine M., Jessica A. Talamas, and Martin Hetzer. “Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa.” <i>Cell</i>. Elsevier, 2010. <a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">https://doi.org/10.1016/j.cell.2010.04.036</a>.","ieee":"C. M. Doucet, J. A. Talamas, and M. Hetzer, “Cell cycle-dependent differences in nuclear pore complex assembly in metazoa,” <i>Cell</i>, vol. 141, no. 6. Elsevier, pp. 1030–1041, 2010.","apa":"Doucet, C. M., Talamas, J. A., &#38; Hetzer, M. (2010). Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">https://doi.org/10.1016/j.cell.2010.04.036</a>","ama":"Doucet CM, Talamas JA, Hetzer M. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. <i>Cell</i>. 2010;141(6):1030-1041. doi:<a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">10.1016/j.cell.2010.04.036</a>"},"year":"2010","language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"month":"06","oa_version":"Published Version","publication":"Cell","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2010.04.036","open_access":"1"}],"oa":1,"publication_identifier":{"issn":["0092-8674"]},"date_published":"2010-06-11T00:00:00Z","type":"journal_article"},{"quality_controlled":"1","page":"372-383","publisher":"Elsevier","article_type":"original","scopus_import":"1","_id":"11102","pmid":1,"issue":"3","author":[{"first_name":"Maya","last_name":"Capelson","full_name":"Capelson, Maya"},{"last_name":"Liang","first_name":"Yun","full_name":"Liang, Yun"},{"last_name":"Schulte","first_name":"Roberta","full_name":"Schulte, Roberta"},{"last_name":"Mair","first_name":"William","full_name":"Mair, William"},{"full_name":"Wagner, Ulrich","first_name":"Ulrich","last_name":"Wagner"},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"date_created":"2022-04-07T07:53:36Z","article_processing_charge":"No","publication_status":"published","intvolume":"       140","title":"Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes","volume":140,"extern":"1","citation":{"ieee":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, and M. Hetzer, “Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes,” <i>Cell</i>, vol. 140, no. 3. Elsevier, pp. 372–383, 2010.","chicago":"Capelson, Maya, Yun Liang, Roberta Schulte, William Mair, Ulrich Wagner, and Martin Hetzer. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression in Higher Eukaryotes.” <i>Cell</i>. Elsevier, 2010. <a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">https://doi.org/10.1016/j.cell.2009.12.054</a>.","ama":"Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. <i>Cell</i>. 2010;140(3):372-383. doi:<a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">10.1016/j.cell.2009.12.054</a>","apa":"Capelson, M., Liang, Y., Schulte, R., Mair, W., Wagner, U., &#38; Hetzer, M. (2010). Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">https://doi.org/10.1016/j.cell.2009.12.054</a>","ista":"Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. 2010. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell. 140(3), 372–383.","short":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, M. Hetzer, Cell 140 (2010) 372–383.","mla":"Capelson, Maya, et al. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression in Higher Eukaryotes.” <i>Cell</i>, vol. 140, no. 3, Elsevier, 2010, pp. 372–83, doi:<a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">10.1016/j.cell.2009.12.054</a>."},"year":"2010","date_updated":"2022-07-18T08:55:03Z","external_id":{"pmid":["20144761"]},"day":"05","doi":"10.1016/j.cell.2009.12.054","abstract":[{"text":"Nuclear pore complexes have recently been shown to play roles in gene activation; however their potential involvement in metazoan transcription remains unclear. Here we show that the nucleoporins Sec13, Nup98, and Nup88, as well as a group of FG-repeat nucleoporins, bind to the Drosophila genome at functionally distinct loci that often do not represent nuclear envelope contact sites. Whereas Nup88 localizes to silent loci, Sec13, Nup98, and a subset of FG-repeat nucleoporins bind to developmentally regulated genes undergoing transcription induction. Strikingly, RNAi-mediated knockdown of intranuclear Sec13 and Nup98 specifically inhibits transcription of their target genes and prevents efficient reactivation of transcription after heat shock, suggesting an essential role of NPC components in regulating complex gene expression programs of multicellular organisms.","lang":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"publication":"Cell","oa_version":"Published Version","month":"02","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2009.12.054"}],"status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","type":"journal_article","date_published":"2010-02-05T00:00:00Z","publication_identifier":{"issn":["0092-8674"]},"oa":1},{"volume":285,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","extern":"1","publication_identifier":{"issn":["0021-9258","1083-351X"]},"day":"19","doi":"10.1074/jbc.m109.061168","abstract":[{"text":"β2-microglobulin (β2m), the light chain of class I major histocompatibility complex, is responsible for the dialysis-related amyloidosis and, in patients undergoing long term dialysis, the full-length and chemically unmodified β2m converts into amyloid fibrils. The protein, belonging to the immunoglobulin superfamily, in common to other members of this family, experiences during its folding a long-lived intermediate associated to the trans-to-cis isomerization of Pro-32 that has been addressed as the precursor of the amyloid fibril formation. In this respect, previous studies on the W60G β2m mutant, showing that the lack of Trp-60 prevents fibril formation in mild aggregating condition, prompted us to reinvestigate the refolding kinetics of wild type and W60G β2m at atomic resolution by real-time NMR. The analysis, conducted at ambient temperature by the band selective flip angle short transient real-time two-dimensional NMR techniques and probing the β2m states every 15 s, revealed a more complex folding energy landscape than previously reported for wild type β2m, involving more than a single intermediate species, and shedding new light into the fibrillogenic pathway. Moreover, a significant difference in the kinetic scheme previously characterized by optical spectroscopic methods was discovered for the W60G β2m mutant.","lang":"eng"}],"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.","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>.","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.","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","date_updated":"2021-01-12T08:19:31Z","type":"journal_article","date_published":"2010-02-19T00:00:00Z","publisher":"American Society for Biochemistry & Molecular Biology","article_type":"original","quality_controlled":"1","page":"5827-5835","keyword":["Cell Biology","Biochemistry","Molecular Biology"],"language":[{"iso":"eng"}],"article_processing_charge":"No","date_created":"2020-09-18T10:11:23Z","oa_version":"None","publication_status":"published","intvolume":"       285","title":"Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR","month":"02","publication":"Journal of Biological Chemistry","_id":"8473","issue":"8","author":[{"last_name":"Corazza","first_name":"Alessandra","full_name":"Corazza, Alessandra"},{"full_name":"Rennella, Enrico","first_name":"Enrico","last_name":"Rennella"},{"last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"last_name":"Mimmi","first_name":"Maria Chiara","full_name":"Mimmi, Maria Chiara"},{"first_name":"Thomas","last_name":"Cutuil","full_name":"Cutuil, Thomas"},{"first_name":"Sara","last_name":"Raimondi","full_name":"Raimondi, Sara"},{"full_name":"Giorgetti, Sofia","first_name":"Sofia","last_name":"Giorgetti"},{"first_name":"Federico","last_name":"Fogolari","full_name":"Fogolari, Federico"},{"first_name":"Paolo","last_name":"Viglino","full_name":"Viglino, Paolo"},{"first_name":"Lucio","last_name":"Frydman","full_name":"Frydman, Lucio"},{"full_name":"Gal, Maayan","last_name":"Gal","first_name":"Maayan"},{"first_name":"Vittorio","last_name":"Bellotti","full_name":"Bellotti, Vittorio"},{"full_name":"Brutscher, Bernhard","last_name":"Brutscher","first_name":"Bernhard"},{"first_name":"Gennaro","last_name":"Esposito","full_name":"Esposito, Gennaro"}]},{"issue":"14","author":[{"id":"e0164712-22ee-11ed-b12a-d80fcdf35958","orcid":"0000-0002-4008-1234","full_name":"Feng, Xiaoqi","first_name":"Xiaoqi","last_name":"Feng"},{"last_name":"Dickinson","first_name":"Hugh G.","full_name":"Dickinson, Hugh G."}],"scopus_import":"1","_id":"12199","pmid":1,"intvolume":"       137","title":"Tapetal cell fate, lineage and proliferation in the Arabidopsis anther","department":[{"_id":"XiFe"}],"article_processing_charge":"No","date_created":"2023-01-16T09:21:54Z","publication_status":"published","quality_controlled":"1","page":"2409-2416","article_type":"original","publisher":"The Company of Biologists","external_id":{"pmid":["20570940"]},"year":"2010","citation":{"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>.","short":"X. Feng, H.G. Dickinson, Development 137 (2010) 2409–2416.","ista":"Feng X, Dickinson HG. 2010. Tapetal cell fate, lineage and proliferation in the Arabidopsis anther. Development. 137(14), 2409–2416.","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>","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.","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>."},"date_updated":"2023-05-08T10:57:11Z","abstract":[{"lang":"eng","text":"The four microsporangia of the flowering plant anther develop from archesporial cells in the L2 of the primordium. Within each microsporangium, developing microsporocytes are surrounded by concentric monolayers of tapetal, middle layer and endothecial cells. How this intricate array of tissues, each containing relatively few cells, is established in an organ possessing no formal meristems is poorly understood. We describe here the pivotal role of the LRR receptor kinase EXCESS MICROSPOROCYTES 1 (EMS1) in forming the monolayer of tapetal nurse cells in Arabidopsis. Unusually for plants, tapetal cells are specified very early in development, and are subsequently stimulated to proliferate by a receptor-like kinase (RLK) complex that includes EMS1. Mutations in members of this EMS1 signalling complex and its putative ligand result in male-sterile plants in which tapetal initials fail to proliferate. Surprisingly, these cells continue to develop, isolated at the locular periphery. Mutant and wild-type microsporangia expand at similar rates and the ‘tapetal’ space at the periphery of mutant locules becomes occupied by microsporocytes. However, induction of late expression of EMS1 in the few tapetal initials in ems1 plants results in their proliferation to generate a functional tapetum, and this proliferation suppresses microsporocyte number. Our experiments also show that integrity of the tapetal monolayer is crucial for the maintenance of the polarity of divisions within it. This unexpected autonomy of the tapetal ‘lineage’ is discussed in the context of tissue development in complex plant organs, where constancy in size, shape and cell number is crucial."}],"day":"15","doi":"10.1242/dev.049320","extern":"1","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).","publication":"Development","month":"07","oa_version":"None","keyword":["Developmental Biology","Molecular Biology","Anther Tapetum","Arabidopsis","Cell Fate Establishment","EMS1","Reproductive Cell Lineage"],"language":[{"iso":"eng"}],"type":"journal_article","date_published":"2010-07-15T00:00:00Z","publication_identifier":{"issn":["1477-9129","0950-1991"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public"},{"keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"language":[{"iso":"eng"}],"month":"11","oa_version":"Published Version","publication":"Developmental Cell","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"url":"https://doi.org/10.1016/j.devcel.2009.10.007","open_access":"1"}],"oa":1,"publication_identifier":{"issn":["1534-5807"]},"type":"journal_article","date_published":"2009-11-17T00:00:00Z","article_type":"review","publisher":"Elsevier","quality_controlled":"1","page":"606-616","intvolume":"        17","title":"Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes","date_created":"2022-04-07T07:53:45Z","article_processing_charge":"No","publication_status":"published","issue":"5","author":[{"first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"last_name":"Wente","first_name":"Susan R.","full_name":"Wente, Susan R."}],"scopus_import":"1","pmid":1,"_id":"11103","extern":"1","volume":17,"abstract":[{"text":"Over the last decade, the nuclear envelope (NE) has emerged as a key component in the organization and function of the nuclear genome. As many as 100 different proteins are thought to specifically localize to this double membrane that separates the cytoplasm and the nucleoplasm of eukaryotic cells. Selective portals through the NE are formed at sites where the inner and outer nuclear membranes are fused, and the coincident assembly of ∼30 proteins into nuclear pore complexes occurs. These nuclear pore complexes are essential for the control of nucleocytoplasmic exchange. Many of the NE and nuclear pore proteins are thought to play crucial roles in gene regulation and thus are increasingly linked to human diseases.","lang":"eng"}],"day":"17","doi":"10.1016/j.devcel.2009.10.007","external_id":{"pmid":["19922866"]},"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","date_updated":"2022-07-18T08:55:01Z"},{"page":"697-705","quality_controlled":"1","article_type":"original","publisher":"EMBO","author":[{"full_name":"Capelson, Maya","last_name":"Capelson","first_name":"Maya"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W"}],"issue":"7","_id":"11105","pmid":1,"scopus_import":"1","title":"The role of nuclear pores in gene regulation, development and disease","intvolume":"        10","publication_status":"published","date_created":"2022-04-07T07:54:06Z","article_processing_charge":"No","extern":"1","volume":10,"external_id":{"pmid":["19543230"]},"date_updated":"2022-07-18T08:42:44Z","year":"2009","citation":{"ista":"Capelson M, Hetzer M. 2009. The role of nuclear pores in gene regulation, development and disease. EMBO reports. 10(7), 697–705.","short":"M. Capelson, M. Hetzer, EMBO Reports 10 (2009) 697–705.","mla":"Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation, Development and Disease.” <i>EMBO Reports</i>, vol. 10, no. 7, EMBO, 2009, pp. 697–705, doi:<a href=\"https://doi.org/10.1038/embor.2009.147\">10.1038/embor.2009.147</a>.","chicago":"Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation, Development and Disease.” <i>EMBO Reports</i>. EMBO, 2009. <a href=\"https://doi.org/10.1038/embor.2009.147\">https://doi.org/10.1038/embor.2009.147</a>.","ieee":"M. Capelson and M. Hetzer, “The role of nuclear pores in gene regulation, development and disease,” <i>EMBO reports</i>, vol. 10, no. 7. EMBO, pp. 697–705, 2009.","apa":"Capelson, M., &#38; Hetzer, M. (2009). The role of nuclear pores in gene regulation, development and disease. <i>EMBO Reports</i>. EMBO. <a href=\"https://doi.org/10.1038/embor.2009.147\">https://doi.org/10.1038/embor.2009.147</a>","ama":"Capelson M, Hetzer M. The role of nuclear pores in gene regulation, development and disease. <i>EMBO reports</i>. 2009;10(7):697-705. doi:<a href=\"https://doi.org/10.1038/embor.2009.147\">10.1038/embor.2009.147</a>"},"abstract":[{"text":"Nuclear-pore complexes (NPCs) are large protein channels that span the nuclear envelope (NE), which is a double membrane that encloses the nuclear genome of eukaryotes. Each of the typically 2,000–4,000 pores in the NE of vertebrate cells is composed of multiple copies of 30 different proteins known as nucleoporins. The evolutionarily conserved NPC proteins have the well-characterized function of mediating the transport of molecules between the nucleoplasm and the cytoplasm. Mutations in nucleoporins are often linked to specific developmental defects and disease, and the resulting phenotypes are usually interpreted as the consequences of perturbed nuclear transport activity. However, recent evidence suggests that NPCs have additional functions in chromatin organization and gene regulation, some of which might be independent of nuclear transport. Here, we review the transport-dependent and transport-independent roles of NPCs in the regulation of nuclear function and gene expression.","lang":"eng"}],"doi":"10.1038/embor.2009.147","day":"01","language":[{"iso":"eng"}],"keyword":["Genetics","Molecular Biology","Biochemistry"],"publication":"EMBO reports","month":"07","oa_version":"Published Version","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/embor.2009.176"}]},"status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/embor.2009.147"}],"date_published":"2009-07-01T00:00:00Z","type":"journal_article","oa":1,"publication_identifier":{"eissn":["1469-3178"],"issn":["1469-221X"]}},{"external_id":{"pmid":["19167330"]},"citation":{"apa":"D’Angelo, M. A., Raices, M., Panowski, S. H., &#38; Hetzer, M. (2009). Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">https://doi.org/10.1016/j.cell.2008.11.037</a>","ama":"D’Angelo MA, Raices M, Panowski SH, Hetzer M. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. <i>Cell</i>. 2009;136(2):284-295. doi:<a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">10.1016/j.cell.2008.11.037</a>","chicago":"D’Angelo, Maximiliano A., Marcela Raices, Siler H. Panowski, and Martin Hetzer. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” <i>Cell</i>. Elsevier, 2009. <a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">https://doi.org/10.1016/j.cell.2008.11.037</a>.","ieee":"M. A. D’Angelo, M. Raices, S. H. Panowski, and M. Hetzer, “Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells,” <i>Cell</i>, vol. 136, no. 2. Elsevier, pp. 284–295, 2009.","mla":"D’Angelo, Maximiliano A., et al. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” <i>Cell</i>, vol. 136, no. 2, Elsevier, 2009, pp. 284–95, doi:<a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">10.1016/j.cell.2008.11.037</a>.","short":"M.A. D’Angelo, M. Raices, S.H. Panowski, M. Hetzer, Cell 136 (2009) 284–295.","ista":"D’Angelo MA, Raices M, Panowski SH, Hetzer M. 2009. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell. 136(2), 284–295."},"year":"2009","date_updated":"2022-07-18T08:55:29Z","abstract":[{"lang":"eng","text":"In dividing cells, nuclear pore complexes (NPCs) disassemble during mitosis and reassemble into the newly forming nuclei. However, the fate of nuclear pores in postmitotic cells is unknown. Here, we show that NPCs, unlike other nuclear structures, do not turn over in differentiated cells. While a subset of NPC components, like Nup153 and Nup50, are continuously exchanged, scaffold nucleoporins, like the Nup107/160 complex, are extremely long-lived and remain incorporated in the nuclear membrane during the entire cellular life span. Besides the lack of nucleoporin expression and NPC turnover, we discovered an age-related deterioration of NPCs, leading to an increase in nuclear permeability and the leaking of cytoplasmic proteins into the nucleus. Our finding that nuclear “leakiness” is dramatically accelerated during aging and that a subset of nucleoporins is oxidatively damaged in old cells suggests that the accumulation of damage at the NPC might be a crucial aging event."}],"day":"23","doi":"10.1016/j.cell.2008.11.037","extern":"1","volume":136,"issue":"2","author":[{"full_name":"D'Angelo, Maximiliano A.","first_name":"Maximiliano A.","last_name":"D'Angelo"},{"first_name":"Marcela","last_name":"Raices","full_name":"Raices, Marcela"},{"full_name":"Panowski, Siler H.","last_name":"Panowski","first_name":"Siler H."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"scopus_import":"1","_id":"11108","pmid":1,"intvolume":"       136","title":"Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells","article_processing_charge":"No","date_created":"2022-04-07T07:54:52Z","publication_status":"published","quality_controlled":"1","page":"284-295","article_type":"original","publisher":"Elsevier","type":"journal_article","date_published":"2009-01-23T00:00:00Z","oa":1,"publication_identifier":{"issn":["0092-8674"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2008.11.037"}],"publication":"Cell","month":"01","oa_version":"Published Version","keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}]},{"intvolume":"       380","month":"07","title":"Folding of the KIX domain: Characterization of the equilibrium analog of a folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy","date_created":"2020-09-18T10:12:29Z","article_processing_charge":"No","oa_version":"None","publication_status":"published","issue":"4","author":[{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul"},{"first_name":"Bernhard","last_name":"Brutscher","full_name":"Brutscher, Bernhard"},{"last_name":"Konrat","first_name":"Robert","full_name":"Konrat, Robert"},{"first_name":"Martin","last_name":"Tollinger","full_name":"Tollinger, Martin"}],"publication":"Journal of Molecular Biology","_id":"8480","article_type":"original","publisher":"Elsevier","keyword":["Molecular Biology"],"language":[{"iso":"eng"}],"quality_controlled":"1","page":"726-741","abstract":[{"text":"The KIX domain of the transcription co-activator CBP is a three-helix bundle protein that folds via rapid accumulation of an intermediate state, followed by a slower folding phase. Recent NMR relaxation dispersion studies revealed the presence of a low-populated (excited) state of KIX that exists in equilibrium with the natively folded form under non-denaturing conditions, and likely represents the equilibrium analog of the folding intermediate. Here, we combine amide hydrogen/deuterium exchange measurements using rapid NMR data acquisition techniques with backbone 15N and 13C relaxation dispersion experiments to further investigate the equilibrium folding of the KIX domain. Residual structure within the folding intermediate is detected by both methods, and their combination enables reliable quantification of the amount of persistent residual structure. Three well-defined folding subunits are found, which display variable stability and correspond closely to the individual helices in the native state. While two of the three helices (α2 and α3) are partially formed in the folding intermediate (to ∼ 50% and ∼ 80%, respectively, at 20 °C), the third helix is disordered. The observed helical content within the excited state exceeds the helical propensities predicted for the corresponding peptide regions, suggesting that the two helices are weakly mutually stabilized, while methyl 13C relaxation dispersion data indicate that a defined packing arrangement is unlikely. Temperature-dependent experiments reveal that the largest enthalpy and entropy changes along the folding reaction occur during the final transition from the intermediate to the native state. Our experimental data are consistent with a folding mechanism where helices α2 and α3 form rapidly, although to different extents, while helix α1 consolidates only as folding proceeds to complete the native state-structure.","lang":"eng"}],"publication_identifier":{"issn":["0022-2836"]},"day":"18","doi":"10.1016/j.jmb.2008.05.040","type":"journal_article","date_published":"2008-07-18T00:00:00Z","citation":{"mla":"Schanda, Paul, et al. “Folding of the KIX Domain: Characterization of the Equilibrium Analog of a Folding Intermediate Using 15N/13C Relaxation Dispersion and Fast 1H/2H Amide Exchange NMR Spectroscopy.” <i>Journal of Molecular Biology</i>, vol. 380, no. 4, Elsevier, 2008, pp. 726–41, doi:<a href=\"https://doi.org/10.1016/j.jmb.2008.05.040\">10.1016/j.jmb.2008.05.040</a>.","short":"P. Schanda, B. Brutscher, R. Konrat, M. Tollinger, Journal of Molecular Biology 380 (2008) 726–741.","ista":"Schanda P, Brutscher B, Konrat R, Tollinger M. 2008. Folding of the KIX domain: Characterization of the equilibrium analog of a folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy. Journal of Molecular Biology. 380(4), 726–741.","ama":"Schanda P, Brutscher B, Konrat R, Tollinger M. Folding of the KIX domain: Characterization of the equilibrium analog of a folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy. <i>Journal of Molecular Biology</i>. 2008;380(4):726-741. doi:<a href=\"https://doi.org/10.1016/j.jmb.2008.05.040\">10.1016/j.jmb.2008.05.040</a>","apa":"Schanda, P., Brutscher, B., Konrat, R., &#38; Tollinger, M. (2008). Folding of the KIX domain: Characterization of the equilibrium analog of a folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2008.05.040\">https://doi.org/10.1016/j.jmb.2008.05.040</a>","ieee":"P. Schanda, B. Brutscher, R. Konrat, and M. Tollinger, “Folding of the KIX domain: Characterization of the equilibrium analog of a folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy,” <i>Journal of Molecular Biology</i>, vol. 380, no. 4. Elsevier, pp. 726–741, 2008.","chicago":"Schanda, Paul, Bernhard Brutscher, Robert Konrat, and Martin Tollinger. “Folding of the KIX Domain: Characterization of the Equilibrium Analog of a Folding Intermediate Using 15N/13C Relaxation Dispersion and Fast 1H/2H Amide Exchange NMR Spectroscopy.” <i>Journal of Molecular Biology</i>. Elsevier, 2008. <a href=\"https://doi.org/10.1016/j.jmb.2008.05.040\">https://doi.org/10.1016/j.jmb.2008.05.040</a>."},"year":"2008","date_updated":"2021-01-12T08:19:34Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","extern":"1","volume":380},{"volume":380,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","extern":"1","day":"04","publication_identifier":{"issn":["0022-2836"]},"doi":"10.1016/j.jmb.2008.05.017","abstract":[{"text":"The copK gene is localized on the pMOL30 plasmid of Cupriavidus metallidurans CH34 within the complex cop cluster of genes, for which 21 genes have been identified. The expression of the corresponding periplasmic CopK protein is strongly upregulated in the presence of copper, leading to a high periplasmic accumulation. The structure and metal-binding properties of CopK were investigated by NMR and mass spectrometry. The protein is dimeric in the apo state with a dissociation constant in the range of 10- 5 M estimated from analytical ultracentrifugation. Mass spectrometry revealed that CopK has two high-affinity Cu(I)-binding sites per monomer with different Cu(I) affinities. Binding of Cu(II) was observed but appeared to be non-specific. The solution structure of apo-CopK revealed an all-β fold formed of two β-sheets in perpendicular orientation with an unstructured C-terminal tail. The dimer interface is formed by the surface of the C-terminal β-sheet. Binding of the first Cu(I)-ion induces a major structural modification involving dissociation of the dimeric apo-protein. Backbone chemical shifts determined for the 1Cu(I)-bound form confirm the conservation of the N-terminal β-sheet, while the last strand of the C-terminal sheet appears in slow conformational exchange. We hypothesize that the partial disruption of the C-terminal β-sheet is related to dimer dissociation. NH-exchange data acquired on the apo-protein are consistent with a lower thermodynamic stability of the C-terminal sheet. CopK contains seven methionine residues, five of which appear highly conserved. Chemical shift data suggest implication of two or three methionines (Met54, Met38, Met28) in the first Cu(I) site. Addition of a second Cu(I) ion further increases protein plasticity. Comparison of the structural and metal-binding properties of CopK with other periplasmic copper-binding proteins reveals two conserved features within these functionally related proteins: the all-β fold and the methionine-rich Cu(I)-binding site.","lang":"eng"}],"year":"2008","citation":{"mla":"Bersch, Beate, et al. “Molecular Structure and Metal-Binding Properties of the Periplasmic CopK Protein Expressed in Cupriavidus Metallidurans CH34 during Copper Challenge.” <i>Journal of Molecular Biology</i>, vol. 380, no. 2, Elsevier, 2008, pp. 386–403, doi:<a href=\"https://doi.org/10.1016/j.jmb.2008.05.017\">10.1016/j.jmb.2008.05.017</a>.","short":"B. Bersch, A. Favier, P. Schanda, S. van Aelst, T. Vallaeys, J. Covès, M. Mergeay, R. Wattiez, Journal of Molecular Biology 380 (2008) 386–403.","ista":"Bersch B, Favier A, Schanda P, van Aelst S, Vallaeys T, Covès J, Mergeay M, Wattiez R. 2008. Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge. Journal of Molecular Biology. 380(2), 386–403.","apa":"Bersch, B., Favier, A., Schanda, P., van Aelst, S., Vallaeys, T., Covès, J., … Wattiez, R. (2008). Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2008.05.017\">https://doi.org/10.1016/j.jmb.2008.05.017</a>","ama":"Bersch B, Favier A, Schanda P, et al. Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge. <i>Journal of Molecular Biology</i>. 2008;380(2):386-403. doi:<a href=\"https://doi.org/10.1016/j.jmb.2008.05.017\">10.1016/j.jmb.2008.05.017</a>","ieee":"B. Bersch <i>et al.</i>, “Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge,” <i>Journal of Molecular Biology</i>, vol. 380, no. 2. Elsevier, pp. 386–403, 2008.","chicago":"Bersch, Beate, Adrien Favier, Paul Schanda, Sébastien van Aelst, Tatiana Vallaeys, Jacques Covès, Max Mergeay, and Ruddy Wattiez. “Molecular Structure and Metal-Binding Properties of the Periplasmic CopK Protein Expressed in Cupriavidus Metallidurans CH34 during Copper Challenge.” <i>Journal of Molecular Biology</i>. Elsevier, 2008. <a href=\"https://doi.org/10.1016/j.jmb.2008.05.017\">https://doi.org/10.1016/j.jmb.2008.05.017</a>."},"date_updated":"2021-01-12T08:19:34Z","type":"journal_article","date_published":"2008-07-04T00:00:00Z","publisher":"Elsevier","article_type":"original","quality_controlled":"1","page":"386-403","keyword":["Molecular Biology"],"language":[{"iso":"eng"}],"article_processing_charge":"No","date_created":"2020-09-18T10:12:37Z","oa_version":"None","publication_status":"published","intvolume":"       380","month":"07","title":"Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge","publication":"Journal of Molecular Biology","_id":"8481","issue":"2","author":[{"last_name":"Bersch","first_name":"Beate","full_name":"Bersch, Beate"},{"full_name":"Favier, Adrien","last_name":"Favier","first_name":"Adrien"},{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"full_name":"van Aelst, Sébastien","last_name":"van Aelst","first_name":"Sébastien"},{"first_name":"Tatiana","last_name":"Vallaeys","full_name":"Vallaeys, Tatiana"},{"first_name":"Jacques","last_name":"Covès","full_name":"Covès, Jacques"},{"full_name":"Mergeay, Max","first_name":"Max","last_name":"Mergeay"},{"last_name":"Wattiez","first_name":"Ruddy","full_name":"Wattiez, Ruddy"}]},{"author":[{"last_name":"Franz","first_name":"Cerstin","full_name":"Franz, Cerstin"},{"full_name":"Walczak, Rudolf","last_name":"Walczak","first_name":"Rudolf"},{"full_name":"Yavuz, Sevil","last_name":"Yavuz","first_name":"Sevil"},{"first_name":"Rachel","last_name":"Santarella","full_name":"Santarella, Rachel"},{"last_name":"Gentzel","first_name":"Marc","full_name":"Gentzel, Marc"},{"last_name":"Askjaer","first_name":"Peter","full_name":"Askjaer, Peter"},{"full_name":"Galy, Vincent","first_name":"Vincent","last_name":"Galy"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"},{"first_name":"Iain W","last_name":"Mattaj","full_name":"Mattaj, Iain W"},{"last_name":"Antonin","first_name":"Wolfram","full_name":"Antonin, Wolfram"}],"issue":"2","_id":"11116","pmid":1,"scopus_import":"1","title":"MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly","intvolume":"         8","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:56:13Z","page":"165-172","quality_controlled":"1","article_type":"original","publisher":"EMBO","external_id":{"pmid":["17235358"]},"date_updated":"2022-07-18T08:56:40Z","year":"2007","citation":{"chicago":"Franz, Cerstin, Rudolf Walczak, Sevil Yavuz, Rachel Santarella, Marc Gentzel, Peter Askjaer, Vincent Galy, Martin Hetzer, Iain W Mattaj, and Wolfram Antonin. “MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins to Chromatin and Postmitotic Nuclear Pore Complex Assembly.” <i>EMBO Reports</i>. EMBO, 2007. <a href=\"https://doi.org/10.1038/sj.embor.7400889\">https://doi.org/10.1038/sj.embor.7400889</a>.","ieee":"C. Franz <i>et al.</i>, “MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly,” <i>EMBO reports</i>, vol. 8, no. 2. EMBO, pp. 165–172, 2007.","ama":"Franz C, Walczak R, Yavuz S, et al. MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. <i>EMBO reports</i>. 2007;8(2):165-172. doi:<a href=\"https://doi.org/10.1038/sj.embor.7400889\">10.1038/sj.embor.7400889</a>","apa":"Franz, C., Walczak, R., Yavuz, S., Santarella, R., Gentzel, M., Askjaer, P., … Antonin, W. (2007). MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. <i>EMBO Reports</i>. EMBO. <a href=\"https://doi.org/10.1038/sj.embor.7400889\">https://doi.org/10.1038/sj.embor.7400889</a>","ista":"Franz C, Walczak R, Yavuz S, Santarella R, Gentzel M, Askjaer P, Galy V, Hetzer M, Mattaj IW, Antonin W. 2007. MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO reports. 8(2), 165–172.","short":"C. Franz, R. Walczak, S. Yavuz, R. Santarella, M. Gentzel, P. Askjaer, V. Galy, M. Hetzer, I.W. Mattaj, W. Antonin, EMBO Reports 8 (2007) 165–172.","mla":"Franz, Cerstin, et al. “MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins to Chromatin and Postmitotic Nuclear Pore Complex Assembly.” <i>EMBO Reports</i>, vol. 8, no. 2, EMBO, 2007, pp. 165–72, doi:<a href=\"https://doi.org/10.1038/sj.embor.7400889\">10.1038/sj.embor.7400889</a>."},"abstract":[{"lang":"eng","text":"The metazoan nuclear envelope (NE) breaks down and re-forms during each cell cycle. Nuclear pore complexes (NPCs), which allow nucleocytoplasmic transport during interphase, assemble into the re-forming NE at the end of mitosis. Using in vitro NE assembly, we show that the vertebrate homologue of MEL-28 (maternal effect lethal), a recently discovered NE component in Caenorhabditis elegans, functions in postmitotic NPC assembly. MEL-28 interacts with the Nup107–160 complex (Nup for nucleoporin), an important building block of the NPC, and is essential for the recruitment of the Nup107–160 complex to chromatin. We suggest that MEL-28 acts as a seeding point for NPC assembly."}],"doi":"10.1038/sj.embor.7400889","day":"19","extern":"1","volume":8,"publication":"EMBO reports","month":"01","oa_version":"Published Version","language":[{"iso":"eng"}],"keyword":["Genetics","Molecular Biology","Biochemistry"],"date_published":"2007-01-19T00:00:00Z","type":"journal_article","oa":1,"publication_identifier":{"eissn":["1469-3178"],"issn":["1469-221X"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/sj.embor.7400889"}]},{"language":[{"iso":"eng"}],"keyword":["Cell Biology","Cellular and Molecular Neuroscience","Pharmacology","Molecular Biology","Molecular Medicine"],"publication":"Cellular and Molecular Life Sciences","month":"01","oa_version":"None","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","date_published":"2006-01-02T00:00:00Z","type":"journal_article","publication_identifier":{"eissn":["1420-9071"],"issn":["1420-682X"]},"page":"316-332","quality_controlled":"1","article_type":"review","publisher":"Springer Nature","author":[{"full_name":"D’Angelo, M. A.","last_name":"D’Angelo","first_name":"M. 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":"3","pmid":1,"_id":"11117","scopus_import":"1","title":"The role of the nuclear envelope in cellular organization","intvolume":"        63","publication_status":"published","date_created":"2022-04-07T07:56:22Z","article_processing_charge":"No","extern":"1","volume":63,"external_id":{"pmid":["16389459"]},"date_updated":"2022-07-18T08:56:58Z","year":"2006","citation":{"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.","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.","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>","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>"},"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."}],"doi":"10.1007/s00018-005-5361-3","day":"02"},{"language":[{"iso":"eng"}],"keyword":["Endocrinology","Genetics","Molecular Biology","Biochemistry"],"publication":"DNA Sequence","oa_version":"None","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","date_published":"2004-01-01T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["1042-5179"]},"page":"153-158","quality_controlled":"1","publisher":"Informa UK Limited","article_type":"original","pmid":1,"_id":"12203","scopus_import":"1","author":[{"first_name":"Zhihua","last_name":"Liao","full_name":"Liao, Zhihua"},{"full_name":"Chen, Min","last_name":"Chen","first_name":"Min"},{"full_name":"Gong, Yifu","last_name":"Gong","first_name":"Yifu"},{"full_name":"Guo, Liang","first_name":"Liang","last_name":"Guo"},{"first_name":"Qiumin","last_name":"Tan","full_name":"Tan, Qiumin"},{"id":"e0164712-22ee-11ed-b12a-d80fcdf35958","orcid":"0000-0002-4008-1234","full_name":"Feng, Xiaoqi","first_name":"Xiaoqi","last_name":"Feng"},{"last_name":"Sun","first_name":"Xiaofen","full_name":"Sun, Xiaofen"},{"full_name":"Tan, Feng","last_name":"Tan","first_name":"Feng"},{"full_name":"Tang, Kexuan","first_name":"Kexuan","last_name":"Tang"}],"issue":"2","publication_status":"published","article_processing_charge":"No","department":[{"_id":"XiFe"}],"date_created":"2023-01-16T09:24:50Z","title":"A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates the biosynthesis of the key precursor for ginkgolides","intvolume":"        15","acknowledgement":"This study was financially supported by China National High-Tech “863” Program. The authors are very thankful to Dr Li Wang (School of Life Sciences, Fudan University, Shanghai, China) for her kind help with constructing the phylogenetic tree.","volume":15,"extern":"1","date_updated":"2023-05-08T10:58:29Z","year":"2004","citation":{"ista":"Liao Z, Chen M, Gong Y, Guo L, Tan Q, Feng X, Sun X, Tan F, Tang K. 2004. A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates the biosynthesis of the key precursor for ginkgolides. DNA Sequence. 15(2), 153–158.","mla":"Liao, Zhihua, et al. “A New Geranylgeranyl Diphosphate Synthase Gene from Ginkgo Biloba, Which Intermediates the Biosynthesis of the Key Precursor for Ginkgolides.” <i>DNA Sequence</i>, vol. 15, no. 2, Informa UK Limited, 2004, pp. 153–58, doi:<a href=\"https://doi.org/10.1080/10425170410001667348\">10.1080/10425170410001667348</a>.","short":"Z. Liao, M. Chen, Y. Gong, L. Guo, Q. Tan, X. Feng, X. Sun, F. Tan, K. Tang, DNA Sequence 15 (2004) 153–158.","chicago":"Liao, Zhihua, Min Chen, Yifu Gong, Liang Guo, Qiumin Tan, Xiaoqi Feng, Xiaofen Sun, Feng Tan, and Kexuan Tang. “A New Geranylgeranyl Diphosphate Synthase Gene from Ginkgo Biloba, Which Intermediates the Biosynthesis of the Key Precursor for Ginkgolides.” <i>DNA Sequence</i>. Informa UK Limited, 2004. <a href=\"https://doi.org/10.1080/10425170410001667348\">https://doi.org/10.1080/10425170410001667348</a>.","ieee":"Z. Liao <i>et al.</i>, “A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates the biosynthesis of the key precursor for ginkgolides,” <i>DNA Sequence</i>, vol. 15, no. 2. Informa UK Limited, pp. 153–158, 2004.","apa":"Liao, Z., Chen, M., Gong, Y., Guo, L., Tan, Q., Feng, X., … Tang, K. (2004). A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates the biosynthesis of the key precursor for ginkgolides. <i>DNA Sequence</i>. Informa UK Limited. <a href=\"https://doi.org/10.1080/10425170410001667348\">https://doi.org/10.1080/10425170410001667348</a>","ama":"Liao Z, Chen M, Gong Y, et al. A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates the biosynthesis of the key precursor for ginkgolides. <i>DNA Sequence</i>. 2004;15(2):153-158. doi:<a href=\"https://doi.org/10.1080/10425170410001667348\">10.1080/10425170410001667348</a>"},"external_id":{"pmid":["15352294"]},"doi":"10.1080/10425170410001667348","abstract":[{"text":"Geranylgeranyl diphosphate synthase (GGPPS, EC: 2.5.1.29) catalyzes the biosynthesis of geranylgeranyl diphosphate (GGPP), which is a key precursor for ginkgolide biosynthesis. Here we reported for the first time the cloning of a new full-length cDNA encoding GGPPS from the living fossil plant Ginkgo biloba. The full-length cDNA encoding G. biloba GGPPS (designated as GbGGPPS) was 1657bp long and contained a 1176bp open reading frame encoding a 391 amino acid protein. Comparative analysis showed that GbGGPPS possessed a 79 amino acid transit peptide at its N-terminal, which directed GbGGPPS to target to the plastids. Bioinformatic analysis revealed that GbGGPPS was a member of polyprenyltransferases with two highly conserved aspartate-rich motifs like other plant GGPPSs. Phylogenetic tree analysis indicated that plant GGPPSs could be classified into two groups, angiosperm and gymnosperm GGPPSs, while GbGGPPS had closer relationship with gymnosperm plant GGPPSs.","lang":"eng"}]},{"language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"publication":"Cell","month":"04","oa_version":"Published Version","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","date_published":"2003-04-17T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["0092-8674"]},"page":"195-206","quality_controlled":"1","article_type":"original","publisher":"Elsevier","author":[{"full_name":"Walther, Tobias C.","last_name":"Walther","first_name":"Tobias C."},{"first_name":"Annabelle","last_name":"Alves","full_name":"Alves, Annabelle"},{"first_name":"Helen","last_name":"Pickersgill","full_name":"Pickersgill, Helen"},{"first_name":"Isabelle","last_name":"Loı̈odice","full_name":"Loı̈odice, Isabelle"},{"first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"full_name":"Galy, Vincent","first_name":"Vincent","last_name":"Galy"},{"first_name":"Bastian B.","last_name":"Hülsmann","full_name":"Hülsmann, Bastian B."},{"full_name":"Köcher, Thomas","first_name":"Thomas","last_name":"Köcher"},{"first_name":"Matthias","last_name":"Wilm","full_name":"Wilm, Matthias"},{"last_name":"Allen","first_name":"Terry","full_name":"Allen, Terry"},{"first_name":"Iain W.","last_name":"Mattaj","full_name":"Mattaj, Iain W."},{"full_name":"Doye, Valérie","first_name":"Valérie","last_name":"Doye"}],"issue":"2","pmid":1,"_id":"11122","scopus_import":"1","title":"The conserved Nup107-160 complex is critical for nuclear pore complex assembly","intvolume":"       113","publication_status":"published","date_created":"2022-04-07T07:57:10Z","article_processing_charge":"No","extern":"1","volume":113,"external_id":{"pmid":["12705868"]},"date_updated":"2022-07-18T08:57:42Z","year":"2003","citation":{"ista":"Walther TC, Alves A, Pickersgill H, Loı̈odice I, Hetzer M, Galy V, Hülsmann BB, Köcher T, Wilm M, Allen T, Mattaj IW, Doye V. 2003. The conserved Nup107-160 complex is critical for nuclear pore complex assembly. Cell. 113(2), 195–206.","short":"T.C. Walther, A. Alves, H. Pickersgill, I. Loı̈odice, M. Hetzer, V. Galy, B.B. Hülsmann, T. Köcher, M. Wilm, T. Allen, I.W. Mattaj, V. Doye, Cell 113 (2003) 195–206.","mla":"Walther, Tobias C., et al. “The Conserved Nup107-160 Complex Is Critical for Nuclear Pore Complex Assembly.” <i>Cell</i>, vol. 113, no. 2, Elsevier, 2003, pp. 195–206, doi:<a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">10.1016/s0092-8674(03)00235-6</a>.","ieee":"T. C. Walther <i>et al.</i>, “The conserved Nup107-160 complex is critical for nuclear pore complex assembly,” <i>Cell</i>, vol. 113, no. 2. Elsevier, pp. 195–206, 2003.","chicago":"Walther, Tobias C., Annabelle Alves, Helen Pickersgill, Isabelle Loı̈odice, Martin Hetzer, Vincent Galy, Bastian B. Hülsmann, et al. “The Conserved Nup107-160 Complex Is Critical for Nuclear Pore Complex Assembly.” <i>Cell</i>. Elsevier, 2003. <a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">https://doi.org/10.1016/s0092-8674(03)00235-6</a>.","apa":"Walther, T. C., Alves, A., Pickersgill, H., Loı̈odice, I., Hetzer, M., Galy, V., … Doye, V. (2003). The conserved Nup107-160 complex is critical for nuclear pore complex assembly. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">https://doi.org/10.1016/s0092-8674(03)00235-6</a>","ama":"Walther TC, Alves A, Pickersgill H, et al. The conserved Nup107-160 complex is critical for nuclear pore complex assembly. <i>Cell</i>. 2003;113(2):195-206. doi:<a href=\"https://doi.org/10.1016/s0092-8674(03)00235-6\">10.1016/s0092-8674(03)00235-6</a>"},"abstract":[{"text":"Nuclear pore complexes (NPCs) are large multiprotein assemblies that allow traffic between the cytoplasm and the nucleus. During mitosis in higher eukaryotes, the Nuclear Envelope (NE) breaks down and NPCs disassemble. How NPCs reassemble and incorporate into the NE upon mitotic exit is poorly understood. We demonstrate a function for the conserved Nup107-160 complex in this process. Partial in vivo depletion of Nup133 or Nup107 via RNAi in HeLa cells resulted in reduced levels of multiple nucleoporins and decreased NPC density in the NE. Immunodepletion of the entire Nup107-160 complex from in vitro nuclear assembly reactions produced nuclei with a continuous NE but no NPCs. This phenotype was reversible only if Nup107-160 complex was readded before closed NE formation. Depletion also prevented association of FG-repeat nucleoporins with chromatin. We propose a stepwise model in which postmitotic NPC assembly initiates on chromatin via early recruitment of the Nup107-160 complex.","lang":"eng"}],"doi":"10.1016/s0092-8674(03)00235-6","day":"17"},{"pmid":1,"_id":"11124","scopus_import":"1","author":[{"first_name":"Daniel","last_name":"Bilbao-Cortés","full_name":"Bilbao-Cortés, Daniel"},{"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":"Längst, Gernot","last_name":"Längst","first_name":"Gernot"},{"full_name":"Becker, Peter B.","first_name":"Peter B.","last_name":"Becker"},{"full_name":"Mattaj, Iain W.","last_name":"Mattaj","first_name":"Iain W."}],"issue":"13","publication_status":"published","date_created":"2022-04-07T07:57:31Z","article_processing_charge":"No","title":"Ran binds to chromatin by two distinct mechanisms","intvolume":"        12","page":"1151-1156","quality_controlled":"1","publisher":"Elsevier BV","article_type":"letter_note","date_updated":"2022-07-18T08:58:05Z","citation":{"ista":"Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. 2002. Ran binds to chromatin by two distinct mechanisms. Current Biology. 12(13), 1151–1156.","short":"D. Bilbao-Cortés, M. Hetzer, G. Längst, P.B. Becker, I.W. Mattaj, Current Biology 12 (2002) 1151–1156.","mla":"Bilbao-Cortés, Daniel, et al. “Ran Binds to Chromatin by Two Distinct Mechanisms.” <i>Current Biology</i>, vol. 12, no. 13, Elsevier BV, 2002, pp. 1151–56, doi:<a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">10.1016/s0960-9822(02)00927-2</a>.","ieee":"D. Bilbao-Cortés, M. Hetzer, G. Längst, P. B. Becker, and I. W. Mattaj, “Ran binds to chromatin by two distinct mechanisms,” <i>Current Biology</i>, vol. 12, no. 13. Elsevier BV, pp. 1151–1156, 2002.","chicago":"Bilbao-Cortés, Daniel, Martin Hetzer, Gernot Längst, Peter B. Becker, and Iain W. Mattaj. “Ran Binds to Chromatin by Two Distinct Mechanisms.” <i>Current Biology</i>. Elsevier BV, 2002. <a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">https://doi.org/10.1016/s0960-9822(02)00927-2</a>.","apa":"Bilbao-Cortés, D., Hetzer, M., Längst, G., Becker, P. B., &#38; Mattaj, I. W. (2002). Ran binds to chromatin by two distinct mechanisms. <i>Current Biology</i>. Elsevier BV. <a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">https://doi.org/10.1016/s0960-9822(02)00927-2</a>","ama":"Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. Ran binds to chromatin by two distinct mechanisms. <i>Current Biology</i>. 2002;12(13):1151-1156. doi:<a href=\"https://doi.org/10.1016/s0960-9822(02)00927-2\">10.1016/s0960-9822(02)00927-2</a>"},"year":"2002","external_id":{"pmid":["12121625"]},"doi":"10.1016/s0960-9822(02)00927-2","day":"09","abstract":[{"text":"Ran GTPase plays important roles in nucleocytoplasmic transport in interphase [1, 2] and in both spindle formation and nuclear envelope (NE) assembly during mitosis [3, 4, 5]. The latter functions rely on the presence of high local concentrations of GTP-bound Ran near mitotic chromatin [3, 4, 5]. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin [6, 7, 8, 9], but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes. We propose that the Ran binding capacity of chromatin contributes to localized spindle and NE assembly.","lang":"eng"}],"volume":12,"extern":"1","publication":"Current Biology","oa_version":"Published Version","month":"07","language":[{"iso":"eng"}],"keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"date_published":"2002-07-09T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["0960-9822"]},"oa":1,"main_file_link":[{"url":"https://doi.org/10.1016/S0960-9822(02)00927-2","open_access":"1"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public"},{"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)"},"date_published":"2002-02-08T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["0021-9258"]},"oa":1,"file":[{"file_id":"13439","creator":"alisjak","success":1,"relation":"main_file","access_level":"open_access","date_updated":"2023-08-01T12:44:09Z","content_type":"application/pdf","file_name":"2002_JBC_Fuerst.pdf","date_created":"2023-08-01T12:44:09Z","checksum":"13abe20f78eb37ab62beb006f62c69b7","file_size":798920}],"status":"public","user_id":"ea97e931-d5af-11eb-85d4-e6957dddbf17","publication":"Journal of Biological Chemistry","has_accepted_license":"1","oa_version":"Published Version","month":"02","language":[{"iso":"eng"}],"keyword":["Cell Biology","Molecular Biology","Biochemistry"],"date_updated":"2023-08-01T12:55:54Z","citation":{"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>.","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>.","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.","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>"},"year":"2002","external_id":{"pmid":["11706026"]},"doi":"10.1074/jbc.m107372200","day":"08","abstract":[{"lang":"eng","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."}],"volume":277,"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","extern":"1","ddc":["570"],"pmid":1,"_id":"13438","scopus_import":"1","author":[{"last_name":"Fürst","first_name":"Johannes","full_name":"Fürst, Johannes"},{"last_name":"Ritter","first_name":"Markus","full_name":"Ritter, Markus"},{"last_name":"Rudzki","first_name":"Jakob","full_name":"Rudzki, Jakob"},{"full_name":"Danzl, Johann G","orcid":"0000-0001-8559-3973","last_name":"Danzl","first_name":"Johann G","id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Gschwentner, Martin","first_name":"Martin","last_name":"Gschwentner"},{"full_name":"Scandella, Elke","first_name":"Elke","last_name":"Scandella"},{"last_name":"Jakab","first_name":"Martin","full_name":"Jakab, Martin"},{"full_name":"König, Matthias","last_name":"König","first_name":"Matthias"},{"full_name":"Oehl, Bernhard","last_name":"Oehl","first_name":"Bernhard"},{"full_name":"Lang, Florian","last_name":"Lang","first_name":"Florian"},{"first_name":"Peter","last_name":"Deetjen","full_name":"Deetjen, Peter"},{"first_name":"Markus","last_name":"Paulmichl","full_name":"Paulmichl, Markus"}],"issue":"6","publication_status":"published","date_created":"2023-08-01T12:37:50Z","article_processing_charge":"No","title":"ICln Ion channel splice variants in Caenorhabditis elegans","intvolume":"       277","page":"4435-4445","quality_controlled":"1","file_date_updated":"2023-08-01T12:44:09Z","publisher":"Elsevier","article_type":"original"},{"language":[{"iso":"eng"}],"keyword":["Cell Biology","Molecular Biology"],"publication":"Molecular Cell","month":"06","oa_version":"Published Version","status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"url":"https://doi.org/10.1016/S1097-2765(00)80266-X","open_access":"1"}],"date_published":"2000-06-01T00:00:00Z","type":"journal_article","oa":1,"publication_identifier":{"issn":["1097-2765"]},"page":"1013-1024","quality_controlled":"1","article_type":"original","publisher":"Elsevier","author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W"},{"first_name":"Daniel","last_name":"Bilbao-Cortés","full_name":"Bilbao-Cortés, Daniel"},{"last_name":"Walther","first_name":"Tobias C","full_name":"Walther, Tobias C"},{"last_name":"Gruss","first_name":"Oliver J","full_name":"Gruss, Oliver J"},{"first_name":"Iain W","last_name":"Mattaj","full_name":"Mattaj, Iain W"}],"issue":"6","pmid":1,"_id":"11127","scopus_import":"1","title":"GTP hydrolysis by Ran is required for nuclear envelope assembly","intvolume":"         5","publication_status":"published","article_processing_charge":"No","date_created":"2022-04-07T07:57:59Z","extern":"1","volume":5,"external_id":{"pmid":["10911995"]},"date_updated":"2022-07-18T08:58:31Z","year":"2000","citation":{"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>.","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>","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>","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.","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>."},"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"}],"doi":"10.1016/s1097-2765(00)80266-x","day":"01"},{"keyword":["amino acid sequence","article","caenorhabditis elegans","evolution","genetic variability","nonhuman","priority journal","sex determination","Amino Acid Sequence","Animals","Animals","Genetically Modified","Base Sequence","Caenorhabditis","Caenorhabditis elegans","Caenorhabditis elegans Proteins","DNA","Helminth","DNA-Binding Proteins","Evolution","Molecular","Female","Helminth Proteins","Membrane Proteins","Molecular Sequence Data","Mutagenesis","RNA","Messenger","Sequence Homology","Amino Acid","Sex Determination (Analysis)","Transcription Factors","Transgenes","Turner Syndrome","Animalia","Caenorhabditis","Caenorhabditis briggsae","Caenorhabditis elegans","Nematoda"],"language":[{"iso":"eng"}],"publication":"Genetics","month":"10","oa_version":"Published Version","user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","status":"public","main_file_link":[{"open_access":"1","url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1207552/"}],"type":"journal_article","date_published":"1996-10-01T00:00:00Z","oa":1,"publication_identifier":{"issn":["00166731"]},"quality_controlled":"1","page":"587-595","publisher":"Genetics Society of America","issue":"2","author":[{"full_name":"de Bono, Mario","orcid":"0000-0001-8347-0443","last_name":"de Bono","first_name":"Mario","id":"4E3FF80E-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Hodgkin","first_name":"J.","full_name":"Hodgkin, J."}],"pmid":1,"_id":"6161","intvolume":"       144","title":"Evolution of sex determination in Caenorhabditis: Unusually high divergence of tra-1 and its functional consequences","date_created":"2019-03-21T11:50:37Z","publication_status":"published","extern":"1","volume":144,"external_id":{"pmid":["8889522"]},"year":"1996","citation":{"ista":"de Bono M, Hodgkin J. 1996. Evolution of sex determination in Caenorhabditis: Unusually high divergence of tra-1 and its functional consequences. Genetics. 144(2), 587–595.","mla":"de Bono, Mario, and J. Hodgkin. “Evolution of Sex Determination in Caenorhabditis: Unusually High Divergence of Tra-1 and Its Functional Consequences.” <i>Genetics</i>, vol. 144, no. 2, Genetics Society of America, 1996, pp. 587–95.","short":"M. de Bono, J. Hodgkin, Genetics 144 (1996) 587–595.","chicago":"Bono, Mario de, and J. Hodgkin. “Evolution of Sex Determination in Caenorhabditis: Unusually High Divergence of Tra-1 and Its Functional Consequences.” <i>Genetics</i>. Genetics Society of America, 1996.","ieee":"M. de Bono and J. Hodgkin, “Evolution of sex determination in Caenorhabditis: Unusually high divergence of tra-1 and its functional consequences,” <i>Genetics</i>, vol. 144, no. 2. Genetics Society of America, pp. 587–595, 1996.","ama":"de Bono M, Hodgkin J. Evolution of sex determination in Caenorhabditis: Unusually high divergence of tra-1 and its functional consequences. <i>Genetics</i>. 1996;144(2):587-595.","apa":"de Bono, M., &#38; Hodgkin, J. (1996). Evolution of sex determination in Caenorhabditis: Unusually high divergence of tra-1 and its functional consequences. <i>Genetics</i>. Genetics Society of America."},"date_updated":"2021-01-12T08:06:28Z","abstract":[{"lang":"eng","text":"The tra-1 gene is a terminal regulator of somatic sex in Caenorhabditis elegans: high tra-1 activity elicits female development, low tra-1 activity elicits male development. To investigate the function and evolution of tra- 1, we examined the tra-1 gene from the closely related nematode C. briggsae. Ce-tra-1 and Cb-tra-1 are unusually divergent. Each gene generates two transcripts, but only one of these is present in both species. This common transcript encodes TRA-1A, which shows only 44% amino acid identity between the species, a figure much lower than that for previously compared genes. A Cb-tra-1 transgene rescues many tissues of tra-1(null) mutants of C. elegans but not the somatic gonad or germ line. This transgene also causes nongonadal feminization of XO animals, indicating incorrect sexual regulation. Alignment of Ce-TRA-1A and Cb-TRA-1A defined several conserved regions likely to be important for tra-1 function. The phenotype differences between Ce-tra- 1(null) mutants rescued by Cb-tra-1 transgenes and wild-type C. elegans indicate significant divergence of regulatory regions. These molecular and functional studies suggest that evolution of sex determination in nematodes is rapid and genetically complex."}],"day":"01"}]