[{"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-018-04139-2"}],"quality_controlled":"1","_id":"14284","date_updated":"2023-11-07T11:46:12Z","type":"journal_article","article_processing_charge":"No","doi":"10.1038/s41467-018-04139-2","publisher":"Springer Nature","pmid":1,"date_published":"2018-05-04T00:00:00Z","status":"public","publication":"Nature Communications","extern":"1","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"year":"2018","external_id":{"pmid":["29728606"]},"publication_identifier":{"issn":["2041-1723"]},"publication_status":"published","intvolume":"         9","abstract":[{"text":"Pore-forming toxins (PFT) are virulence factors that transform from soluble to membrane-bound states. The Yersinia YaxAB system represents a family of binary α-PFTs with orthologues in human, insect, and plant pathogens, with unknown structures. YaxAB was shown to be cytotoxic and likely involved in pathogenesis, though the molecular basis for its two-component lytic mechanism remains elusive. Here, we present crystal structures of YaxA and YaxB, together with a cryo-electron microscopy map of the YaxAB complex. Our structures reveal a pore predominantly composed of decamers of YaxA–YaxB heterodimers. Both subunits bear membrane-active moieties, but only YaxA is capable of binding to membranes by itself. YaxB can subsequently be recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices. Pore formation can progress by further oligomerization of YaxA–YaxB dimers. Our results allow for a comparison between pore assemblies belonging to the wider ClyA-like family of α-PFTs, highlighting diverse pore architectures.","lang":"eng"}],"volume":9,"date_created":"2023-09-06T12:07:33Z","article_type":"original","scopus_import":"1","day":"04","author":[{"last_name":"Bräuning","full_name":"Bräuning, Bastian","first_name":"Bastian"},{"first_name":"Eva","full_name":"Bertosin, Eva","last_name":"Bertosin"},{"last_name":"Praetorius","full_name":"Praetorius, Florian M","id":"dfec9381-4341-11ee-8fd8-faa02bba7d62","first_name":"Florian M"},{"last_name":"Ihling","full_name":"Ihling, Christian","first_name":"Christian"},{"full_name":"Schatt, Alexandra","last_name":"Schatt","first_name":"Alexandra"},{"full_name":"Adler, Agnes","last_name":"Adler","first_name":"Agnes"},{"full_name":"Richter, Klaus","last_name":"Richter","first_name":"Klaus"},{"first_name":"Andrea","last_name":"Sinz","full_name":"Sinz, Andrea"},{"full_name":"Dietz, Hendrik","last_name":"Dietz","first_name":"Hendrik"},{"full_name":"Groll, Michael","last_name":"Groll","first_name":"Michael"}],"oa_version":"Published Version","title":"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB","citation":{"ista":"Bräuning B, Bertosin E, Praetorius FM, Ihling C, Schatt A, Adler A, Richter K, Sinz A, Dietz H, Groll M. 2018. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. Nature Communications. 9, 1806.","chicago":"Bräuning, Bastian, Eva Bertosin, Florian M Praetorius, Christian Ihling, Alexandra Schatt, Agnes Adler, Klaus Richter, Andrea Sinz, Hendrik Dietz, and Michael Groll. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” <i>Nature Communications</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>.","mla":"Bräuning, Bastian, et al. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” <i>Nature Communications</i>, vol. 9, 1806, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41467-018-04139-2\">10.1038/s41467-018-04139-2</a>.","apa":"Bräuning, B., Bertosin, E., Praetorius, F. M., Ihling, C., Schatt, A., Adler, A., … Groll, M. (2018). Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>","ama":"Bräuning B, Bertosin E, Praetorius FM, et al. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. <i>Nature Communications</i>. 2018;9. doi:<a href=\"https://doi.org/10.1038/s41467-018-04139-2\">10.1038/s41467-018-04139-2</a>","short":"B. Bräuning, E. Bertosin, F.M. Praetorius, C. Ihling, A. Schatt, A. Adler, K. Richter, A. Sinz, H. Dietz, M. Groll, Nature Communications 9 (2018).","ieee":"B. Bräuning <i>et al.</i>, “Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB,” <i>Nature Communications</i>, vol. 9. Springer Nature, 2018."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"language":[{"iso":"eng"}],"article_number":"1806","month":"05"},{"volume":8,"article_type":"original","date_created":"2022-04-07T07:45:50Z","author":[{"first_name":"Abigail","full_name":"Buchwalter, Abigail","last_name":"Buchwalter"},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W"}],"scopus_import":"1","day":"30","oa_version":"Published Version","title":"Nucleolar expansion and elevated protein translation in premature aging","publication_status":"published","publication_identifier":{"issn":["2041-1723"]},"abstract":[{"lang":"eng","text":"Premature aging disorders provide an opportunity to study the mechanisms that drive aging. In Hutchinson-Gilford progeria syndrome (HGPS), a mutant form of the nuclear scaffold protein lamin A distorts nuclei and sequesters nuclear proteins. We sought to investigate protein homeostasis in this disease. Here, we report a widespread increase in protein turnover in HGPS-derived cells compared to normal cells. We determine that global protein synthesis is elevated as a consequence of activated nucleoli and enhanced ribosome biogenesis in HGPS-derived fibroblasts. Depleting normal lamin A or inducing mutant lamin A expression are each sufficient to drive nucleolar expansion. We further show that nucleolar size correlates with donor age in primary fibroblasts derived from healthy individuals and that ribosomal RNA production increases with age, indicating that nucleolar size and activity can serve as aging biomarkers. While limiting ribosome biogenesis extends lifespan in several systems, we show that increased ribosome biogenesis and activity are a hallmark of premature aging."}],"intvolume":"         8","article_number":"328","month":"08","citation":{"ama":"Buchwalter A, Hetzer M. Nucleolar expansion and elevated protein translation in premature aging. <i>Nature Communications</i>. 2017;8. doi:<a href=\"https://doi.org/10.1038/s41467-017-00322-z\">10.1038/s41467-017-00322-z</a>","short":"A. Buchwalter, M. Hetzer, Nature Communications 8 (2017).","ieee":"A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","chicago":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” <i>Nature Communications</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1038/s41467-017-00322-z\">https://doi.org/10.1038/s41467-017-00322-z</a>.","ista":"Buchwalter A, Hetzer M. 2017. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 8, 328.","mla":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” <i>Nature Communications</i>, vol. 8, 328, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/s41467-017-00322-z\">10.1038/s41467-017-00322-z</a>.","apa":"Buchwalter, A., &#38; Hetzer, M. (2017). Nucleolar expansion and elevated protein translation in premature aging. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-017-00322-z\">https://doi.org/10.1038/s41467-017-00322-z</a>"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa":1,"language":[{"iso":"eng"}],"date_updated":"2022-07-18T08:33:03Z","_id":"11065","type":"journal_article","doi":"10.1038/s41467-017-00322-z","article_processing_charge":"No","publisher":"Springer Nature","main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-00322-z","open_access":"1"}],"quality_controlled":"1","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"year":"2017","external_id":{"pmid":["28855503"]},"pmid":1,"date_published":"2017-08-30T00:00:00Z","extern":"1","publication":"Nature Communications","status":"public"},{"article_number":"15651","month":"06","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"apa":"Walt, S. G., Bhargava Ram, N., Atala, M., Shvetsov-Shilovski, N. I., von Conta, A., Baykusheva, D. R., … Wörner, H. J. (2017). Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms15651\">https://doi.org/10.1038/ncomms15651</a>","mla":"Walt, Samuel G., et al. “Dynamics of Valence-Shell Electrons and Nuclei Probed by Strong-Field Holography and Rescattering.” <i>Nature Communications</i>, vol. 8, 15651, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/ncomms15651\">10.1038/ncomms15651</a>.","chicago":"Walt, Samuel G., Niraghatam Bhargava Ram, Marcos Atala, Nikolay I Shvetsov-Shilovski, Aaron von Conta, Denitsa Rangelova Baykusheva, Manfred Lein, and Hans Jakob Wörner. “Dynamics of Valence-Shell Electrons and Nuclei Probed by Strong-Field Holography and Rescattering.” <i>Nature Communications</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1038/ncomms15651\">https://doi.org/10.1038/ncomms15651</a>.","ista":"Walt SG, Bhargava Ram N, Atala M, Shvetsov-Shilovski NI, von Conta A, Baykusheva DR, Lein M, Wörner HJ. 2017. Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. Nature Communications. 8, 15651.","ieee":"S. G. Walt <i>et al.</i>, “Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","short":"S.G. Walt, N. Bhargava Ram, M. Atala, N.I. Shvetsov-Shilovski, A. von Conta, D.R. Baykusheva, M. Lein, H.J. Wörner, Nature Communications 8 (2017).","ama":"Walt SG, Bhargava Ram N, Atala M, et al. Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. <i>Nature Communications</i>. 2017;8. doi:<a href=\"https://doi.org/10.1038/ncomms15651\">10.1038/ncomms15651</a>"},"language":[{"iso":"eng"}],"oa":1,"article_type":"original","date_created":"2023-08-10T06:36:09Z","volume":8,"oa_version":"Published Version","title":"Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering","author":[{"last_name":"Walt","full_name":"Walt, Samuel G.","first_name":"Samuel G."},{"first_name":"Niraghatam","full_name":"Bhargava Ram, Niraghatam","last_name":"Bhargava Ram"},{"first_name":"Marcos","full_name":"Atala, Marcos","last_name":"Atala"},{"first_name":"Nikolay I","full_name":"Shvetsov-Shilovski, Nikolay I","last_name":"Shvetsov-Shilovski"},{"first_name":"Aaron","full_name":"von Conta, Aaron","last_name":"von Conta"},{"last_name":"Baykusheva","id":"71b4d059-2a03-11ee-914d-dfa3beed6530","full_name":"Baykusheva, Denitsa Rangelova","first_name":"Denitsa Rangelova"},{"full_name":"Lein, Manfred","last_name":"Lein","first_name":"Manfred"},{"full_name":"Wörner, Hans Jakob","last_name":"Wörner","first_name":"Hans Jakob"}],"day":"15","scopus_import":"1","publication_identifier":{"eissn":["2041-1723"]},"publication_status":"published","intvolume":"         8","abstract":[{"lang":"eng","text":"Strong-field photoelectron holography and laser-induced electron diffraction (LIED) are two powerful emerging methods for probing the ultrafast dynamics of molecules. However, both of them have remained restricted to static systems and to nuclear dynamics induced by strong-field ionization. Here we extend these promising methods to image purely electronic valence-shell dynamics in molecules using photoelectron holography. In the same experiment, we use LIED and photoelectron holography simultaneously, to observe coupled electronic-rotational dynamics taking place on similar timescales. These results offer perspectives for imaging ultrafast dynamics of molecules on femtosecond to attosecond timescales."}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"external_id":{"pmid":["28643771"]},"year":"2017","date_published":"2017-06-15T00:00:00Z","pmid":1,"status":"public","publication":"Nature Communications","extern":"1","type":"journal_article","date_updated":"2023-08-22T08:26:06Z","_id":"14005","publisher":"Springer Nature","doi":"10.1038/ncomms15651","article_processing_charge":"No","quality_controlled":"1","main_file_link":[{"url":"https://doi.org/10.1038/ncomms15651","open_access":"1"}]},{"intvolume":"         6","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)"},"abstract":[{"lang":"eng","text":"Eukaryotic cells are densely packed with macromolecular complexes and intertwining organelles, continually transported and reshaped. Intriguingly, organelles avoid clashing and entangling with each other in such limited space. Mitochondria form extensive networks constantly remodeled by fission and fusion. Here, we show that mitochondrial fission is triggered by mechanical forces. Mechano-stimulation of mitochondria – via encounter with motile intracellular pathogens, via external pressure applied by an atomic force microscope, or via cell migration across uneven microsurfaces – results in the recruitment of the mitochondrial fission machinery, and subsequent division. We propose that MFF, owing to affinity for narrow mitochondria, acts as a membrane-bound force sensor to recruit the fission machinery to mechanically strained sites. Thus, mitochondria adapt to the environment by sensing and responding to biomechanical cues. Our findings that mechanical triggers can be coupled to biochemical responses in membrane dynamics may explain how organelles orderly cohabit in the crowded cytoplasm."}],"has_accepted_license":"1","publication_identifier":{"issn":["2050-084X"]},"publication_status":"published","file_date_updated":"2021-11-29T09:07:41Z","title":"Mechanical force induces mitochondrial fission","oa_version":"Published Version","author":[{"first_name":"Sebastian Carsten Johannes","full_name":"Helle, Sebastian Carsten Johannes","last_name":"Helle"},{"first_name":"Qian","last_name":"Feng","full_name":"Feng, Qian"},{"full_name":"Aebersold, Mathias J","last_name":"Aebersold","first_name":"Mathias J"},{"full_name":"Hirt, Luca","last_name":"Hirt","first_name":"Luca"},{"first_name":"Raphael R","last_name":"Grüter","full_name":"Grüter, Raphael R"},{"first_name":"Afshin","last_name":"Vahid","full_name":"Vahid, Afshin"},{"last_name":"Sirianni","full_name":"Sirianni, Andrea","first_name":"Andrea"},{"first_name":"Serge","full_name":"Mostowy, Serge","last_name":"Mostowy"},{"first_name":"Jess G","full_name":"Snedeker, Jess G","last_name":"Snedeker"},{"first_name":"Anđela","orcid":"0000-0002-7854-2139","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","full_name":"Šarić, Anđela","last_name":"Šarić"},{"full_name":"Idema, Timon","last_name":"Idema","first_name":"Timon"},{"last_name":"Zambelli","full_name":"Zambelli, Tomaso","first_name":"Tomaso"},{"first_name":"Benoît","last_name":"Kornmann","full_name":"Kornmann, Benoît"}],"day":"09","scopus_import":"1","article_type":"original","date_created":"2021-11-29T08:51:38Z","volume":6,"language":[{"iso":"eng"}],"oa":1,"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","citation":{"mla":"Helle, Sebastian Carsten Johannes, et al. “Mechanical Force Induces Mitochondrial Fission.” <i>ELife</i>, vol. 6, e30292, eLife Sciences Publications, 2017, doi:<a href=\"https://doi.org/10.7554/elife.30292\">10.7554/elife.30292</a>.","apa":"Helle, S. C. J., Feng, Q., Aebersold, M. J., Hirt, L., Grüter, R. R., Vahid, A., … Kornmann, B. (2017). Mechanical force induces mitochondrial fission. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/elife.30292\">https://doi.org/10.7554/elife.30292</a>","chicago":"Helle, Sebastian Carsten Johannes, Qian Feng, Mathias J Aebersold, Luca Hirt, Raphael R Grüter, Afshin Vahid, Andrea Sirianni, et al. “Mechanical Force Induces Mitochondrial Fission.” <i>ELife</i>. eLife Sciences Publications, 2017. <a href=\"https://doi.org/10.7554/elife.30292\">https://doi.org/10.7554/elife.30292</a>.","ista":"Helle SCJ, Feng Q, Aebersold MJ, Hirt L, Grüter RR, Vahid A, Sirianni A, Mostowy S, Snedeker JG, Šarić A, Idema T, Zambelli T, Kornmann B. 2017. Mechanical force induces mitochondrial fission. eLife. 6, e30292.","short":"S.C.J. Helle, Q. Feng, M.J. Aebersold, L. Hirt, R.R. Grüter, A. Vahid, A. Sirianni, S. Mostowy, J.G. Snedeker, A. Šarić, T. Idema, T. Zambelli, B. Kornmann, ELife 6 (2017).","ieee":"S. C. J. Helle <i>et al.</i>, “Mechanical force induces mitochondrial fission,” <i>eLife</i>, vol. 6. eLife Sciences Publications, 2017.","ama":"Helle SCJ, Feng Q, Aebersold MJ, et al. Mechanical force induces mitochondrial fission. <i>eLife</i>. 2017;6. doi:<a href=\"https://doi.org/10.7554/elife.30292\">10.7554/elife.30292</a>"},"month":"11","article_number":"e30292","file":[{"date_updated":"2021-11-29T09:07:41Z","creator":"cchlebak","file_size":6120157,"date_created":"2021-11-29T09:07:41Z","file_id":"10372","access_level":"open_access","content_type":"application/pdf","success":1,"file_name":"2017_eLife_Helle.pdf","checksum":"c35f42dcfb007f6d6c761a27e24c26d3","relation":"main_file"}],"ddc":["572"],"quality_controlled":"1","main_file_link":[{"open_access":"1","url":"https://elifesciences.org/articles/30292"}],"publisher":"eLife Sciences Publications","doi":"10.7554/elife.30292","article_processing_charge":"No","type":"journal_article","date_updated":"2021-11-29T09:28:14Z","_id":"10370","publication":"eLife","extern":"1","status":"public","date_published":"2017-11-09T00:00:00Z","pmid":1,"external_id":{"pmid":["29119945"]},"year":"2017","keyword":["general immunology and microbiology","general biochemistry","genetics and molecular biology","general medicine","general neuroscience"]},{"article_number":"13874","month":"12","citation":{"short":"R.A.H. van de Ven, J.S. de Groot, D. Park, R. van Domselaar, D. de Jong, K. Szuhai, E. van der Wall, O.M. Rueda, H.R. Ali, C. Caldas, P.J. van Diest, M. Hetzer, E. Sahai, P.W.B. Derksen, Nature Communications 7 (2016).","ieee":"R. A. H. van de Ven <i>et al.</i>, “p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis,” <i>Nature Communications</i>, vol. 7. Springer Nature, 2016.","ama":"van de Ven RAH, de Groot JS, Park D, et al. p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. <i>Nature Communications</i>. 2016;7. doi:<a href=\"https://doi.org/10.1038/ncomms13874\">10.1038/ncomms13874</a>","mla":"van de Ven, Robert A. H., et al. “P120-Catenin Prevents Multinucleation through Control of MKLP1-Dependent RhoA Activity during Cytokinesis.” <i>Nature Communications</i>, vol. 7, 13874, Springer Nature, 2016, doi:<a href=\"https://doi.org/10.1038/ncomms13874\">10.1038/ncomms13874</a>.","apa":"van de Ven, R. A. H., de Groot, J. S., Park, D., van Domselaar, R., de Jong, D., Szuhai, K., … Derksen, P. W. B. (2016). p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms13874\">https://doi.org/10.1038/ncomms13874</a>","ista":"van de Ven RAH, de Groot JS, Park D, van Domselaar R, de Jong D, Szuhai K, van der Wall E, Rueda OM, Ali HR, Caldas C, van Diest PJ, Hetzer M, Sahai E, Derksen PWB. 2016. p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. Nature Communications. 7, 13874.","chicago":"Ven, Robert A.H. van de, Jolien S. de Groot, Danielle Park, Robert van Domselaar, Danielle de Jong, Karoly Szuhai, Elsken van der Wall, et al. “P120-Catenin Prevents Multinucleation through Control of MKLP1-Dependent RhoA Activity during Cytokinesis.” <i>Nature Communications</i>. Springer Nature, 2016. <a href=\"https://doi.org/10.1038/ncomms13874\">https://doi.org/10.1038/ncomms13874</a>."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa":1,"language":[{"iso":"eng"}],"volume":7,"date_created":"2022-04-07T07:48:34Z","article_type":"original","scopus_import":"1","day":"22","author":[{"full_name":"van de Ven, Robert A.H.","last_name":"van de Ven","first_name":"Robert A.H."},{"first_name":"Jolien S.","last_name":"de Groot","full_name":"de Groot, Jolien S."},{"first_name":"Danielle","last_name":"Park","full_name":"Park, Danielle"},{"last_name":"van Domselaar","full_name":"van Domselaar, Robert","first_name":"Robert"},{"full_name":"de Jong, Danielle","last_name":"de Jong","first_name":"Danielle"},{"first_name":"Karoly","last_name":"Szuhai","full_name":"Szuhai, Karoly"},{"first_name":"Elsken","last_name":"van der Wall","full_name":"van der Wall, Elsken"},{"first_name":"Oscar M.","last_name":"Rueda","full_name":"Rueda, Oscar M."},{"full_name":"Ali, H. Raza","last_name":"Ali","first_name":"H. Raza"},{"first_name":"Carlos","full_name":"Caldas, Carlos","last_name":"Caldas"},{"full_name":"van Diest, Paul J.","last_name":"van Diest","first_name":"Paul J."},{"full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","orcid":"0000-0002-2111-992X"},{"first_name":"Erik","full_name":"Sahai, Erik","last_name":"Sahai"},{"full_name":"Derksen, Patrick W.B.","last_name":"Derksen","first_name":"Patrick W.B."}],"title":"p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis","oa_version":"Published Version","publication_identifier":{"issn":["2041-1723"]},"publication_status":"published","abstract":[{"text":"Spatiotemporal activation of RhoA and actomyosin contraction underpins cellular adhesion and division. Loss of cell–cell adhesion and chromosomal instability are cardinal events that drive tumour progression. Here, we show that p120-catenin (p120) not only controls cell–cell adhesion, but also acts as a critical regulator of cytokinesis. We find that p120 regulates actomyosin contractility through concomitant binding to RhoA and the centralspindlin component MKLP1, independent of cadherin association. In anaphase, p120 is enriched at the cleavage furrow where it binds MKLP1 to spatially control RhoA GTPase cycling. Binding of p120 to MKLP1 during cytokinesis depends on the N-terminal coiled-coil domain of p120 isoform 1A. Importantly, clinical data show that loss of p120 expression is a common event in breast cancer that strongly correlates with multinucleation and adverse patient survival. In summary, our study identifies p120 loss as a driver event of chromosomal instability in cancer.\r\n","lang":"eng"}],"intvolume":"         7","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"year":"2016","related_material":{"link":[{"url":"https://doi.org/10.1038/ncomms16030","relation":"erratum"}]},"external_id":{"pmid":["28004812"]},"pmid":1,"date_published":"2016-12-22T00:00:00Z","publication":"Nature Communications","extern":"1","status":"public","_id":"11072","date_updated":"2022-07-18T08:34:32Z","type":"journal_article","article_processing_charge":"No","doi":"10.1038/ncomms13874","publisher":"Springer Nature","main_file_link":[{"url":"https://doi.org/10.1038/ncomms13874","open_access":"1"}],"quality_controlled":"1"},{"publication_identifier":{"issn":["0092-8674"]},"publication_status":"published","abstract":[{"lang":"eng","text":"Human cancer cells bear complex chromosome rearrangements that can be potential drivers of cancer development. However, the molecular mechanisms underlying these rearrangements have been unclear. Zhang et al. use a new technique combining live-cell imaging and single-cell sequencing to demonstrate that chromosomes mis-segregated to micronuclei frequently undergo chromothripsis-like rearrangements in the subsequent cell cycle."}],"intvolume":"       161","volume":161,"date_created":"2022-04-07T07:48:49Z","article_type":"original","day":"18","scopus_import":"1","author":[{"last_name":"Hatch","full_name":"Hatch, Emily M.","first_name":"Emily M."},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W"}],"title":"Linking micronuclei to chromosome fragmentation","oa_version":"Published Version","citation":{"ista":"Hatch EM, Hetzer M. 2015. Linking micronuclei to chromosome fragmentation. Cell. 161(7), 1502–1504.","chicago":"Hatch, Emily M., and Martin Hetzer. “Linking Micronuclei to Chromosome Fragmentation.” <i>Cell</i>. Elsevier, 2015. <a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">https://doi.org/10.1016/j.cell.2015.06.005</a>.","mla":"Hatch, Emily M., and Martin Hetzer. “Linking Micronuclei to Chromosome Fragmentation.” <i>Cell</i>, vol. 161, no. 7, Elsevier, 2015, pp. 1502–04, doi:<a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">10.1016/j.cell.2015.06.005</a>.","apa":"Hatch, E. M., &#38; Hetzer, M. (2015). Linking micronuclei to chromosome fragmentation. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">https://doi.org/10.1016/j.cell.2015.06.005</a>","ama":"Hatch EM, Hetzer M. Linking micronuclei to chromosome fragmentation. <i>Cell</i>. 2015;161(7):1502-1504. doi:<a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">10.1016/j.cell.2015.06.005</a>","short":"E.M. Hatch, M. Hetzer, Cell 161 (2015) 1502–1504.","ieee":"E. M. Hatch and M. Hetzer, “Linking micronuclei to chromosome fragmentation,” <i>Cell</i>, vol. 161, no. 7. Elsevier, pp. 1502–1504, 2015."},"issue":"7","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa":1,"language":[{"iso":"eng"}],"month":"06","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2015.06.005"}],"quality_controlled":"1","page":"1502-1504","_id":"11073","date_updated":"2022-07-18T08:34:33Z","type":"journal_article","article_processing_charge":"No","doi":"10.1016/j.cell.2015.06.005","publisher":"Elsevier","pmid":1,"date_published":"2015-06-18T00:00:00Z","extern":"1","status":"public","publication":"Cell","keyword":["General Biochemistry","Genetics and Molecular Biology"],"year":"2015","external_id":{"pmid":["26091034"]}},{"oa":1,"language":[{"iso":"eng"}],"issue":"10","citation":{"chicago":"Hatch, Emily M., and Martin Hetzer. “Chromothripsis.” <i>Current Biology</i>. Elsevier, 2015. <a href=\"https://doi.org/10.1016/j.cub.2015.02.033\">https://doi.org/10.1016/j.cub.2015.02.033</a>.","ista":"Hatch EM, Hetzer M. 2015. Chromothripsis. Current Biology. 25(10), PR397-R399.","apa":"Hatch, E. M., &#38; Hetzer, M. (2015). Chromothripsis. <i>Current Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cub.2015.02.033\">https://doi.org/10.1016/j.cub.2015.02.033</a>","mla":"Hatch, Emily M., and Martin Hetzer. “Chromothripsis.” <i>Current Biology</i>, vol. 25, no. 10, Elsevier, 2015, pp. PR397-R399, doi:<a href=\"https://doi.org/10.1016/j.cub.2015.02.033\">10.1016/j.cub.2015.02.033</a>.","ama":"Hatch EM, Hetzer M. Chromothripsis. <i>Current Biology</i>. 2015;25(10):PR397-R399. doi:<a href=\"https://doi.org/10.1016/j.cub.2015.02.033\">10.1016/j.cub.2015.02.033</a>","ieee":"E. M. Hatch and M. Hetzer, “Chromothripsis,” <i>Current Biology</i>, vol. 25, no. 10. Elsevier, pp. PR397-R399, 2015.","short":"E.M. Hatch, M. Hetzer, Current Biology 25 (2015) PR397-R399."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","month":"05","intvolume":"        25","publication_identifier":{"issn":["0960-9822"]},"publication_status":"published","author":[{"last_name":"Hatch","full_name":"Hatch, Emily M.","first_name":"Emily M."},{"last_name":"HETZER","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X"}],"scopus_import":"1","day":"18","oa_version":"Published Version","title":"Chromothripsis","volume":25,"article_type":"original","date_created":"2022-04-07T07:49:00Z","extern":"1","status":"public","publication":"Current Biology","pmid":1,"date_published":"2015-05-18T00:00:00Z","year":"2015","external_id":{"pmid":["25989073"]},"keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"page":"PR397-R399","main_file_link":[{"url":"https://doi.org/10.1016/j.cub.2015.02.033","open_access":"1"}],"quality_controlled":"1","doi":"10.1016/j.cub.2015.02.033","article_processing_charge":"No","publisher":"Elsevier","date_updated":"2022-07-18T08:34:34Z","_id":"11074","type":"journal_article"},{"language":[{"iso":"eng"}],"publication":"Nature Communications","status":"public","extern":"1","citation":{"short":"P. Ma, Y. Xue, N. Coquelle, J.D. Haller, T. Yuwen, I. Ayala, O. Mikhailovskii, D. Willbold, J.-P. Colletier, N.R. Skrynnikov, P. Schanda, Nature Communications 6 (2015).","ieee":"P. Ma <i>et al.</i>, “Observing the overall rocking motion of a protein in a crystal,” <i>Nature Communications</i>, vol. 6. Springer Nature, 2015.","ama":"Ma P, Xue Y, Coquelle N, et al. Observing the overall rocking motion of a protein in a crystal. <i>Nature Communications</i>. 2015;6. doi:<a href=\"https://doi.org/10.1038/ncomms9361\">10.1038/ncomms9361</a>","mla":"Ma, Peixiang, et al. “Observing the Overall Rocking Motion of a Protein in a Crystal.” <i>Nature Communications</i>, vol. 6, 8361, Springer Nature, 2015, doi:<a href=\"https://doi.org/10.1038/ncomms9361\">10.1038/ncomms9361</a>.","apa":"Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., … Schanda, P. (2015). Observing the overall rocking motion of a protein in a crystal. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms9361\">https://doi.org/10.1038/ncomms9361</a>","ista":"Ma P, Xue Y, Coquelle N, Haller JD, Yuwen T, Ayala I, Mikhailovskii O, Willbold D, Colletier J-P, Skrynnikov NR, Schanda P. 2015. Observing the overall rocking motion of a protein in a crystal. Nature Communications. 6, 8361.","chicago":"Ma, Peixiang, Yi Xue, Nicolas Coquelle, Jens D. Haller, Tairan Yuwen, Isabel Ayala, Oleg Mikhailovskii, et al. “Observing the Overall Rocking Motion of a Protein in a Crystal.” <i>Nature Communications</i>. Springer Nature, 2015. <a href=\"https://doi.org/10.1038/ncomms9361\">https://doi.org/10.1038/ncomms9361</a>."},"date_published":"2015-10-05T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2015","month":"10","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"article_number":"8361","intvolume":"         6","abstract":[{"lang":"eng","text":"The large majority of three-dimensional structures of biological macromolecules have been determined by X-ray diffraction of crystalline samples. High-resolution structure determination crucially depends on the homogeneity of the protein crystal. Overall ‘rocking’ motion of molecules in the crystal is expected to influence diffraction quality, and such motion may therefore affect the process of solving crystal structures. Yet, so far overall molecular motion has not directly been observed in protein crystals, and the timescale of such dynamics remains unclear. Here we use solid-state NMR, X-ray diffraction methods and μs-long molecular dynamics simulations to directly characterize the rigid-body motion of a protein in different crystal forms. For ubiquitin crystals investigated in this study we determine the range of possible correlation times of rocking motion, 0.1–100 μs. The amplitude of rocking varies from one crystal form to another and is correlated with the resolution obtainable in X-ray diffraction experiments."}],"quality_controlled":"1","publication_status":"published","publication_identifier":{"issn":["2041-1723"]},"doi":"10.1038/ncomms9361","author":[{"first_name":"Peixiang","full_name":"Ma, Peixiang","last_name":"Ma"},{"full_name":"Xue, Yi","last_name":"Xue","first_name":"Yi"},{"last_name":"Coquelle","full_name":"Coquelle, Nicolas","first_name":"Nicolas"},{"first_name":"Jens D.","last_name":"Haller","full_name":"Haller, Jens D."},{"last_name":"Yuwen","full_name":"Yuwen, Tairan","first_name":"Tairan"},{"first_name":"Isabel","full_name":"Ayala, Isabel","last_name":"Ayala"},{"full_name":"Mikhailovskii, Oleg","last_name":"Mikhailovskii","first_name":"Oleg"},{"last_name":"Willbold","full_name":"Willbold, Dieter","first_name":"Dieter"},{"last_name":"Colletier","full_name":"Colletier, Jacques-Philippe","first_name":"Jacques-Philippe"},{"first_name":"Nikolai R.","last_name":"Skrynnikov","full_name":"Skrynnikov, Nikolai R."},{"last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","first_name":"Paul"}],"article_processing_charge":"No","day":"05","oa_version":"Published Version","publisher":"Springer Nature","title":"Observing the overall rocking motion of a protein in a crystal","date_updated":"2021-01-12T08:19:24Z","_id":"8456","volume":6,"type":"journal_article","article_type":"original","date_created":"2020-09-18T10:07:36Z"},{"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"external_id":{"pmid":["25940229"]},"year":"2015","date_published":"2015-05-05T00:00:00Z","pmid":1,"extern":"1","status":"public","publication":"Nature Communications","type":"journal_article","date_updated":"2023-08-22T08:52:56Z","_id":"14016","publisher":"Springer Nature","doi":"10.1038/ncomms8039","article_processing_charge":"No","quality_controlled":"1","main_file_link":[{"url":"https://doi.org/10.1038/ncomms8039","open_access":"1"}],"article_number":"7039","month":"05","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"chicago":"Kraus, P. M., O. I. Tolstikhin, Denitsa Rangelova Baykusheva, A. Rupenyan, J. Schneider, C. Z. Bisgaard, T. Morishita, F. Jensen, L. B. Madsen, and H. J. Wörner. “Observation of Laser-Induced Electronic Structure in Oriented Polyatomic Molecules.” <i>Nature Communications</i>. Springer Nature, 2015. <a href=\"https://doi.org/10.1038/ncomms8039\">https://doi.org/10.1038/ncomms8039</a>.","ista":"Kraus PM, Tolstikhin OI, Baykusheva DR, Rupenyan A, Schneider J, Bisgaard CZ, Morishita T, Jensen F, Madsen LB, Wörner HJ. 2015. Observation of laser-induced electronic structure in oriented polyatomic molecules. Nature Communications. 6, 7039.","apa":"Kraus, P. M., Tolstikhin, O. I., Baykusheva, D. R., Rupenyan, A., Schneider, J., Bisgaard, C. Z., … Wörner, H. J. (2015). Observation of laser-induced electronic structure in oriented polyatomic molecules. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms8039\">https://doi.org/10.1038/ncomms8039</a>","mla":"Kraus, P. M., et al. “Observation of Laser-Induced Electronic Structure in Oriented Polyatomic Molecules.” <i>Nature Communications</i>, vol. 6, 7039, Springer Nature, 2015, doi:<a href=\"https://doi.org/10.1038/ncomms8039\">10.1038/ncomms8039</a>.","ama":"Kraus PM, Tolstikhin OI, Baykusheva DR, et al. Observation of laser-induced electronic structure in oriented polyatomic molecules. <i>Nature Communications</i>. 2015;6. doi:<a href=\"https://doi.org/10.1038/ncomms8039\">10.1038/ncomms8039</a>","ieee":"P. M. Kraus <i>et al.</i>, “Observation of laser-induced electronic structure in oriented polyatomic molecules,” <i>Nature Communications</i>, vol. 6. Springer Nature, 2015.","short":"P.M. Kraus, O.I. Tolstikhin, D.R. Baykusheva, A. Rupenyan, J. Schneider, C.Z. Bisgaard, T. Morishita, F. Jensen, L.B. Madsen, H.J. Wörner, Nature Communications 6 (2015)."},"language":[{"iso":"eng"}],"oa":1,"article_type":"original","date_created":"2023-08-10T06:38:01Z","volume":6,"title":"Observation of laser-induced electronic structure in oriented polyatomic molecules","oa_version":"Published Version","author":[{"full_name":"Kraus, P. M.","last_name":"Kraus","first_name":"P. M."},{"first_name":"O. I.","last_name":"Tolstikhin","full_name":"Tolstikhin, O. I."},{"first_name":"Denitsa Rangelova","full_name":"Baykusheva, Denitsa Rangelova","id":"71b4d059-2a03-11ee-914d-dfa3beed6530","last_name":"Baykusheva"},{"first_name":"A.","last_name":"Rupenyan","full_name":"Rupenyan, A."},{"last_name":"Schneider","full_name":"Schneider, J.","first_name":"J."},{"full_name":"Bisgaard, C. Z.","last_name":"Bisgaard","first_name":"C. Z."},{"full_name":"Morishita, T.","last_name":"Morishita","first_name":"T."},{"last_name":"Jensen","full_name":"Jensen, F.","first_name":"F."},{"full_name":"Madsen, L. B.","last_name":"Madsen","first_name":"L. B."},{"first_name":"H. J.","last_name":"Wörner","full_name":"Wörner, H. J."}],"scopus_import":"1","day":"05","publication_identifier":{"eissn":["2041-1723"]},"publication_status":"published","intvolume":"         6","abstract":[{"lang":"eng","text":"All attosecond time-resolved measurements have so far relied on the use of intense near-infrared laser pulses. In particular, attosecond streaking, laser-induced electron diffraction and high-harmonic generation all make use of non-perturbative light–matter interactions. Remarkably, the effect of the strong laser field on the studied sample has often been neglected in previous studies. Here we use high-harmonic spectroscopy to measure laser-induced modifications of the electronic structure of molecules. We study high-harmonic spectra of spatially oriented CH3F and CH3Br as generic examples of polar polyatomic molecules. We accurately measure intensity ratios of even and odd-harmonic orders, and of the emission from aligned and unaligned molecules. We show that these robust observables reveal a substantial modification of the molecular electronic structure by the external laser field. Our insights offer new challenges and opportunities for a range of emerging strong-field attosecond spectroscopies."}]},{"doi":"10.1016/j.cell.2014.02.004","article_processing_charge":"No","publisher":"Elsevier","date_updated":"2022-07-18T08:44:33Z","_id":"11080","type":"journal_article","page":"868-869","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2014.02.004"}],"quality_controlled":"1","year":"2014","external_id":{"pmid":["24581486"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"extern":"1","status":"public","publication":"Cell","pmid":1,"date_published":"2014-02-27T00:00:00Z","author":[{"full_name":"Buchwalter, Abigail","last_name":"Buchwalter","first_name":"Abigail"},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"scopus_import":"1","day":"27","oa_version":"Published Version","title":"Nuclear pores set the speed limit for mitosis","volume":156,"article_type":"original","date_created":"2022-04-07T07:50:04Z","intvolume":"       156","abstract":[{"text":"The spindle assembly checkpoint prevents separation of sister chromatids until each kinetochore is attached to the mitotic spindle. Rodriguez-Bravo et al. report that the nuclear pore complex scaffolds spindle assembly checkpoint signaling in interphase, providing a store of inhibitory signals that limits the speed of the subsequent mitosis.","lang":"eng"}],"publication_status":"published","publication_identifier":{"issn":["0092-8674"]},"month":"02","oa":1,"language":[{"iso":"eng"}],"issue":"5","citation":{"mla":"Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit for Mitosis.” <i>Cell</i>, vol. 156, no. 5, Elsevier, 2014, pp. 868–69, doi:<a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">10.1016/j.cell.2014.02.004</a>.","apa":"Buchwalter, A., &#38; Hetzer, M. (2014). Nuclear pores set the speed limit for mitosis. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">https://doi.org/10.1016/j.cell.2014.02.004</a>","chicago":"Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit for Mitosis.” <i>Cell</i>. Elsevier, 2014. <a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">https://doi.org/10.1016/j.cell.2014.02.004</a>.","ista":"Buchwalter A, Hetzer M. 2014. Nuclear pores set the speed limit for mitosis. Cell. 156(5), 868–869.","short":"A. Buchwalter, M. Hetzer, Cell 156 (2014) 868–869.","ieee":"A. Buchwalter and M. Hetzer, “Nuclear pores set the speed limit for mitosis,” <i>Cell</i>, vol. 156, no. 5. Elsevier, pp. 868–869, 2014.","ama":"Buchwalter A, Hetzer M. Nuclear pores set the speed limit for mitosis. <i>Cell</i>. 2014;156(5):868-869. doi:<a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">10.1016/j.cell.2014.02.004</a>"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd"},{"external_id":{"pmid":["24709950"]},"year":"2014","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"status":"public","publication":"Nature Communications","extern":"1","date_published":"2014-04-07T00:00:00Z","pmid":1,"publisher":"Springer Nature","doi":"10.1038/ncomms4588","article_processing_charge":"No","type":"journal_article","date_updated":"2023-08-08T07:28:10Z","_id":"13402","quality_controlled":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms4588"}],"month":"04","article_number":"3588","language":[{"iso":"eng"}],"oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"chicago":"Kundu, Pintu K., Gregory L. Olsen, Vladimir Kiss, and Rafal Klajn. “Nanoporous Frameworks Exhibiting Multiple Stimuli Responsiveness.” <i>Nature Communications</i>. Springer Nature, 2014. <a href=\"https://doi.org/10.1038/ncomms4588\">https://doi.org/10.1038/ncomms4588</a>.","ista":"Kundu PK, Olsen GL, Kiss V, Klajn R. 2014. Nanoporous frameworks exhibiting multiple stimuli responsiveness. Nature Communications. 5, 3588.","apa":"Kundu, P. K., Olsen, G. L., Kiss, V., &#38; Klajn, R. (2014). Nanoporous frameworks exhibiting multiple stimuli responsiveness. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms4588\">https://doi.org/10.1038/ncomms4588</a>","mla":"Kundu, Pintu K., et al. “Nanoporous Frameworks Exhibiting Multiple Stimuli Responsiveness.” <i>Nature Communications</i>, vol. 5, 3588, Springer Nature, 2014, doi:<a href=\"https://doi.org/10.1038/ncomms4588\">10.1038/ncomms4588</a>.","ama":"Kundu PK, Olsen GL, Kiss V, Klajn R. Nanoporous frameworks exhibiting multiple stimuli responsiveness. <i>Nature Communications</i>. 2014;5. doi:<a href=\"https://doi.org/10.1038/ncomms4588\">10.1038/ncomms4588</a>","ieee":"P. K. Kundu, G. L. Olsen, V. Kiss, and R. Klajn, “Nanoporous frameworks exhibiting multiple stimuli responsiveness,” <i>Nature Communications</i>, vol. 5. Springer Nature, 2014.","short":"P.K. Kundu, G.L. Olsen, V. Kiss, R. Klajn, Nature Communications 5 (2014)."},"oa_version":"Published Version","title":"Nanoporous frameworks exhibiting multiple stimuli responsiveness","author":[{"first_name":"Pintu K.","full_name":"Kundu, Pintu K.","last_name":"Kundu"},{"first_name":"Gregory L.","last_name":"Olsen","full_name":"Olsen, Gregory L."},{"first_name":"Vladimir","full_name":"Kiss, Vladimir","last_name":"Kiss"},{"full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn","first_name":"Rafal"}],"scopus_import":"1","day":"07","article_type":"original","date_created":"2023-08-01T09:46:27Z","volume":5,"abstract":[{"text":"Nanoporous frameworks are polymeric materials built from rigid molecules, which give rise to their nanoporous structures with applications in gas sorption and storage, catalysis and others. Conceptually new applications could emerge, should these beneficial properties be manipulated by external stimuli in a reversible manner. One approach to render nanoporous frameworks responsive to external signals would be to immobilize molecular switches within their nanopores. Although the majority of molecular switches require conformational freedom to isomerize, and switching in the solid state is prohibited, the nanopores may provide enough room for the switches to efficiently isomerize. Here we describe two families of nanoporous materials incorporating the spiropyran molecular switch. These materials exhibit a variety of interesting properties, including reversible photochromism and acidochromism under solvent-free conditions, light-controlled capture and release of metal ions, as well reversible chromism induced by solvation/desolvation.","lang":"eng"}],"intvolume":"         5","publication_identifier":{"eissn":["2041-1723"]},"publication_status":"published"},{"article_type":"original","date_created":"2022-04-07T07:50:51Z","volume":154,"oa_version":"Published Version","title":"Catastrophic nuclear envelope collapse in cancer cell micronuclei","author":[{"full_name":"Hatch, Emily M.","last_name":"Hatch","first_name":"Emily M."},{"first_name":"Andrew H.","full_name":"Fischer, Andrew H.","last_name":"Fischer"},{"full_name":"Deerinck, Thomas J.","last_name":"Deerinck","first_name":"Thomas J."},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","last_name":"HETZER"}],"scopus_import":"1","day":"03","publication_status":"published","publication_identifier":{"issn":["0092-8674"]},"intvolume":"       154","abstract":[{"text":"During mitotic exit, missegregated chromosomes can recruit their own nuclear envelope (NE) to form micronuclei (MN). MN have reduced functioning compared to primary nuclei in the same cell, although the two compartments appear to be structurally comparable. Here we show that over 60% of MN undergo an irreversible loss of compartmentalization during interphase due to NE collapse. This disruption of the MN, which is induced by defects in nuclear lamina assembly, drastically reduces nuclear functions and can trigger massive DNA damage. MN disruption is associated with chromatin compaction and invasion of endoplasmic reticulum (ER) tubules into the chromatin. We identified disrupted MN in both major subtypes of human non-small-cell lung cancer, suggesting that disrupted MN could be a useful objective biomarker for genomic instability in solid tumors. Our study shows that NE collapse is a key event underlying MN dysfunction and establishes a link between aberrant NE organization and aneuploidy.","lang":"eng"}],"month":"07","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","issue":"1","citation":{"mla":"Hatch, Emily M., et al. “Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei.” <i>Cell</i>, vol. 154, no. 1, Elsevier, 2013, pp. 47–60, doi:<a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">10.1016/j.cell.2013.06.007</a>.","apa":"Hatch, E. M., Fischer, A. H., Deerinck, T. J., &#38; Hetzer, M. (2013). Catastrophic nuclear envelope collapse in cancer cell micronuclei. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">https://doi.org/10.1016/j.cell.2013.06.007</a>","ista":"Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. 2013. Catastrophic nuclear envelope collapse in cancer cell micronuclei. Cell. 154(1), 47–60.","chicago":"Hatch, Emily M., Andrew H. Fischer, Thomas J. Deerinck, and Martin Hetzer. “Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei.” <i>Cell</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">https://doi.org/10.1016/j.cell.2013.06.007</a>.","short":"E.M. Hatch, A.H. Fischer, T.J. Deerinck, M. Hetzer, Cell 154 (2013) 47–60.","ieee":"E. M. Hatch, A. H. Fischer, T. J. Deerinck, and M. Hetzer, “Catastrophic nuclear envelope collapse in cancer cell micronuclei,” <i>Cell</i>, vol. 154, no. 1. Elsevier, pp. 47–60, 2013.","ama":"Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. Catastrophic nuclear envelope collapse in cancer cell micronuclei. <i>Cell</i>. 2013;154(1):47-60. doi:<a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">10.1016/j.cell.2013.06.007</a>"},"language":[{"iso":"eng"}],"oa":1,"type":"journal_article","date_updated":"2022-07-18T08:45:47Z","_id":"11085","publisher":"Elsevier","doi":"10.1016/j.cell.2013.06.007","article_processing_charge":"No","quality_controlled":"1","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2013.06.007","open_access":"1"}],"page":"47-60","keyword":["General Biochemistry","Genetics and Molecular Biology"],"external_id":{"pmid":["23827674"]},"year":"2013","date_published":"2013-07-03T00:00:00Z","pmid":1,"status":"public","extern":"1","publication":"Cell"},{"oa_version":"Published Version","title":"Identification of long-lived proteins reveals exceptional stability of essential cellular structures","author":[{"first_name":"Brandon H.","full_name":"Toyama, Brandon H.","last_name":"Toyama"},{"full_name":"Savas, Jeffrey N.","last_name":"Savas","first_name":"Jeffrey N."},{"first_name":"Sung Kyu","last_name":"Park","full_name":"Park, Sung Kyu"},{"first_name":"Michael S.","last_name":"Harris","full_name":"Harris, Michael S."},{"first_name":"Nicholas T.","last_name":"Ingolia","full_name":"Ingolia, Nicholas T."},{"first_name":"John R.","last_name":"Yates","full_name":"Yates, John R."},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"}],"day":"29","scopus_import":"1","article_type":"original","date_created":"2022-04-07T07:51:08Z","volume":154,"abstract":[{"lang":"eng","text":"Intracellular proteins with long lifespans have recently been linked to age-dependent defects, ranging from decreased fertility to the functional decline of neurons. Why long-lived proteins exist in metabolically active cellular environments and how they are maintained over time remains poorly understood. Here, we provide a system-wide identification of proteins with exceptional lifespans in the rat brain. These proteins are inefficiently replenished despite being translated robustly throughout adulthood. Using nucleoporins as a paradigm for long-term protein persistence, we found that nuclear pore complexes (NPCs) are maintained over a cell’s life through slow but finite exchange of even its most stable subcomplexes. This maintenance is limited, however, as some nucleoporin levels decrease during aging, providing a rationale for the previously observed age-dependent deterioration of NPC function. Our identification of a long-lived proteome reveals cellular components that are at increased risk for damage accumulation, linking long-term protein persistence to the cellular aging process."}],"intvolume":"       154","publication_status":"published","publication_identifier":{"issn":["0092-8674"]},"month":"08","language":[{"iso":"eng"}],"oa":1,"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","issue":"5","citation":{"ama":"Toyama BH, Savas JN, Park SK, et al. Identification of long-lived proteins reveals exceptional stability of essential cellular structures. <i>Cell</i>. 2013;154(5):971-982. doi:<a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">10.1016/j.cell.2013.07.037</a>","short":"B.H. Toyama, J.N. Savas, S.K. Park, M.S. Harris, N.T. Ingolia, J.R. Yates, M. Hetzer, Cell 154 (2013) 971–982.","ieee":"B. H. Toyama <i>et al.</i>, “Identification of long-lived proteins reveals exceptional stability of essential cellular structures,” <i>Cell</i>, vol. 154, no. 5. Elsevier, pp. 971–982, 2013.","ista":"Toyama BH, Savas JN, Park SK, Harris MS, Ingolia NT, Yates JR, Hetzer M. 2013. Identification of long-lived proteins reveals exceptional stability of essential cellular structures. Cell. 154(5), 971–982.","chicago":"Toyama, Brandon H., Jeffrey N. Savas, Sung Kyu Park, Michael S. Harris, Nicholas T. Ingolia, John R. Yates, and Martin Hetzer. “Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures.” <i>Cell</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">https://doi.org/10.1016/j.cell.2013.07.037</a>.","mla":"Toyama, Brandon H., et al. “Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures.” <i>Cell</i>, vol. 154, no. 5, Elsevier, 2013, pp. 971–82, doi:<a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">10.1016/j.cell.2013.07.037</a>.","apa":"Toyama, B. H., Savas, J. N., Park, S. K., Harris, M. S., Ingolia, N. T., Yates, J. R., &#38; Hetzer, M. (2013). Identification of long-lived proteins reveals exceptional stability of essential cellular structures. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">https://doi.org/10.1016/j.cell.2013.07.037</a>"},"publisher":"Elsevier","doi":"10.1016/j.cell.2013.07.037","article_processing_charge":"No","type":"journal_article","date_updated":"2022-07-18T08:50:47Z","_id":"11087","page":"971-982","quality_controlled":"1","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2013.07.037","open_access":"1"}],"external_id":{"pmid":["23993091"]},"year":"2013","keyword":["General Biochemistry","Genetics and Molecular Biology"],"extern":"1","publication":"Cell","status":"public","date_published":"2013-08-29T00:00:00Z","pmid":1},{"abstract":[{"lang":"eng","text":"Nuclear export of mRNAs is thought to occur exclusively through nuclear pore complexes. In this issue of Cell, Speese et al. identify an alternate pathway for mRNA export in muscle cells where ribonucleoprotein complexes involved in forming neuromuscular junctions transit the nuclear envelope by fusing with and budding through the nuclear membrane."}],"intvolume":"       149","publication_identifier":{"issn":["0092-8674"]},"publication_status":"published","author":[{"first_name":"Emily M.","last_name":"Hatch","full_name":"Hatch, Emily M."},{"last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","first_name":"Martin W","orcid":"0000-0002-2111-992X"}],"scopus_import":"1","day":"11","title":"RNP export by nuclear envelope budding","oa_version":"Published Version","volume":149,"article_type":"letter_note","date_created":"2022-04-07T07:51:45Z","oa":1,"language":[{"iso":"eng"}],"issue":"4","citation":{"ama":"Hatch EM, Hetzer M. RNP export by nuclear envelope budding. <i>Cell</i>. 2012;149(4):733-735. doi:<a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">10.1016/j.cell.2012.04.018</a>","short":"E.M. Hatch, M. Hetzer, Cell 149 (2012) 733–735.","ieee":"E. M. Hatch and M. Hetzer, “RNP export by nuclear envelope budding,” <i>Cell</i>, vol. 149, no. 4. Elsevier, pp. 733–735, 2012.","ista":"Hatch EM, Hetzer M. 2012. RNP export by nuclear envelope budding. Cell. 149(4), 733–735.","chicago":"Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.” <i>Cell</i>. Elsevier, 2012. <a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">https://doi.org/10.1016/j.cell.2012.04.018</a>.","mla":"Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.” <i>Cell</i>, vol. 149, no. 4, Elsevier, 2012, pp. 733–35, doi:<a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">10.1016/j.cell.2012.04.018</a>.","apa":"Hatch, E. M., &#38; Hetzer, M. (2012). RNP export by nuclear envelope budding. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">https://doi.org/10.1016/j.cell.2012.04.018</a>"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","month":"05","page":"733-735","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2012.04.018","open_access":"1"}],"quality_controlled":"1","doi":"10.1016/j.cell.2012.04.018","article_processing_charge":"No","publisher":"Elsevier","date_updated":"2022-07-18T08:58:48Z","_id":"11090","type":"journal_article","status":"public","publication":"Cell","extern":"1","pmid":1,"date_published":"2012-05-11T00:00:00Z","year":"2012","external_id":{"pmid":["22579277"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"]},{"doi":"10.1016/j.devcel.2011.11.021","article_processing_charge":"No","publisher":"Elsevier","date_updated":"2022-07-18T08:53:16Z","_id":"11093","type":"journal_article","page":"446-458","main_file_link":[{"url":"https://doi.org/10.1016/j.devcel.2011.11.021","open_access":"1"}],"quality_controlled":"1","year":"2012","external_id":{"pmid":["22264802"]},"keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"status":"public","extern":"1","publication":"Developmental Cell","pmid":1,"date_published":"2012-01-19T00:00:00Z","author":[{"last_name":"D'Angelo","full_name":"D'Angelo, Maximiliano A.","first_name":"Maximiliano A."},{"last_name":"Gomez-Cavazos","full_name":"Gomez-Cavazos, J. Sebastian","first_name":"J. Sebastian"},{"first_name":"Arianna","last_name":"Mei","full_name":"Mei, Arianna"},{"last_name":"Lackner","full_name":"Lackner, Daniel H.","first_name":"Daniel H."},{"full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","first_name":"Martin W"}],"scopus_import":"1","day":"19","oa_version":"Published Version","title":"A change in nuclear pore complex composition regulates cell differentiation","volume":22,"article_type":"original","date_created":"2022-04-07T07:52:10Z","intvolume":"        22","abstract":[{"text":"Nuclear pore complexes (NPCs) are built from ∼30 different proteins called nucleoporins or Nups. Previous studies have shown that several Nups exhibit cell-type-specific expression and that mutations in NPC components result in tissue-specific diseases. Here we show that a specific change in NPC composition is required for both myogenic and neuronal differentiation. The transmembrane nucleoporin Nup210 is absent in proliferating myoblasts and embryonic stem cells (ESCs) but becomes expressed and incorporated into NPCs during cell differentiation. Preventing Nup210 production by RNAi blocks myogenesis and the differentiation of ESCs into neuroprogenitors. We found that the addition of Nup210 to NPCs does not affect nuclear transport but is required for the induction of genes that are essential for cell differentiation. Our results identify a single change in NPC composition as an essential step in cell differentiation and establish a role for Nup210 in gene expression regulation and cell fate determination.","lang":"eng"}],"publication_identifier":{"issn":["1534-5807"]},"publication_status":"published","month":"01","oa":1,"language":[{"iso":"eng"}],"issue":"2","citation":{"ieee":"M. A. D’Angelo, J. S. Gomez-Cavazos, A. Mei, D. H. Lackner, and M. Hetzer, “A change in nuclear pore complex composition regulates cell differentiation,” <i>Developmental Cell</i>, vol. 22, no. 2. Elsevier, pp. 446–458, 2012.","short":"M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental Cell 22 (2012) 446–458.","ama":"D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. A change in nuclear pore complex composition regulates cell differentiation. <i>Developmental Cell</i>. 2012;22(2):446-458. doi:<a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">10.1016/j.devcel.2011.11.021</a>","apa":"D’Angelo, M. A., Gomez-Cavazos, J. S., Mei, A., Lackner, D. H., &#38; Hetzer, M. (2012). A change in nuclear pore complex composition regulates cell differentiation. <i>Developmental Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">https://doi.org/10.1016/j.devcel.2011.11.021</a>","mla":"D’Angelo, Maximiliano A., et al. “A Change in Nuclear Pore Complex Composition Regulates Cell Differentiation.” <i>Developmental Cell</i>, vol. 22, no. 2, Elsevier, 2012, pp. 446–58, doi:<a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">10.1016/j.devcel.2011.11.021</a>.","chicago":"D’Angelo, Maximiliano A., J. Sebastian Gomez-Cavazos, Arianna Mei, Daniel H. Lackner, and Martin Hetzer. “A Change in Nuclear Pore Complex Composition Regulates Cell Differentiation.” <i>Developmental Cell</i>. Elsevier, 2012. <a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">https://doi.org/10.1016/j.devcel.2011.11.021</a>.","ista":"D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. 2012. A change in nuclear pore complex composition regulates cell differentiation. Developmental Cell. 22(2), 446–458."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd"},{"month":"02","citation":{"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>","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.","short":"M. Hetzer, Cold Spring Harbor Perspectives in Biology 2 (2010) a000539–a000539.","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>.","ista":"Hetzer M. 2010. The nuclear envelope. Cold Spring Harbor Perspectives in Biology. 2(3), a000539–a000539.","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>","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>."},"issue":"3","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","language":[{"iso":"eng"}],"volume":2,"date_created":"2022-04-07T07:52:49Z","article_type":"original","scopus_import":"1","day":"03","author":[{"full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","orcid":"0000-0002-2111-992X"}],"title":"The nuclear envelope","oa_version":"None","publication_status":"published","publication_identifier":{"issn":["1943-0264"]},"intvolume":"         2","abstract":[{"lang":"eng","text":"The nuclear envelope (NE) is a highly regulated membrane barrier that separates the nucleus from the cytoplasm in eukaryotic cells. It contains a large number of different proteins that have been implicated in chromatin organization and gene regulation. Although the nuclear membrane enables complex levels of gene expression, it also poses a challenge when it comes to cell division. To allow access of the mitotic spindle to chromatin, the nucleus of metazoans must completely disassemble during mitosis, generating the need to re-establish the nuclear compartment at the end of each cell division. Here, I summarize our current understanding of the dynamic remodeling of the NE during the cell cycle."}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"year":"2010","external_id":{"pmid":["20300205"]},"pmid":1,"date_published":"2010-02-03T00:00:00Z","status":"public","publication":"Cold Spring Harbor Perspectives in Biology","extern":"1","_id":"11097","date_updated":"2022-07-18T08:53:50Z","type":"journal_article","article_processing_charge":"No","doi":"10.1101/cshperspect.a000539","publisher":"Cold Spring Harbor Laboratory","quality_controlled":"1","page":"a000539-a000539"},{"oa":1,"language":[{"iso":"eng"}],"citation":{"short":"C.M. Doucet, J.A. Talamas, M. Hetzer, Cell 141 (2010) 1030–1041.","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.","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>","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>.","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>","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>.","ista":"Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041."},"issue":"6","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","month":"06","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."}],"intvolume":"       141","publication_identifier":{"issn":["0092-8674"]},"publication_status":"published","day":"11","scopus_import":"1","author":[{"last_name":"Doucet","full_name":"Doucet, Christine M.","first_name":"Christine M."},{"first_name":"Jessica A.","last_name":"Talamas","full_name":"Talamas, Jessica A."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W","orcid":"0000-0002-2111-992X"}],"title":"Cell cycle-dependent differences in nuclear pore complex assembly in metazoa","oa_version":"Published Version","volume":141,"date_created":"2022-04-07T07:53:29Z","article_type":"original","extern":"1","status":"public","publication":"Cell","pmid":1,"date_published":"2010-06-11T00:00:00Z","year":"2010","external_id":{"pmid":["20550937"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"page":"1030-1041","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2010.04.036","open_access":"1"}],"quality_controlled":"1","article_processing_charge":"No","doi":"10.1016/j.cell.2010.04.036","publisher":"Elsevier","_id":"11101","date_updated":"2022-07-18T08:54:52Z","type":"journal_article"},{"type":"journal_article","date_updated":"2022-07-18T08:55:03Z","_id":"11102","publisher":"Elsevier","doi":"10.1016/j.cell.2009.12.054","article_processing_charge":"No","quality_controlled":"1","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2009.12.054","open_access":"1"}],"page":"372-383","keyword":["General Biochemistry","Genetics and Molecular Biology"],"external_id":{"pmid":["20144761"]},"year":"2010","date_published":"2010-02-05T00:00:00Z","pmid":1,"publication":"Cell","status":"public","extern":"1","article_type":"original","date_created":"2022-04-07T07:53:36Z","volume":140,"title":"Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes","oa_version":"Published Version","author":[{"last_name":"Capelson","full_name":"Capelson, Maya","first_name":"Maya"},{"last_name":"Liang","full_name":"Liang, Yun","first_name":"Yun"},{"full_name":"Schulte, Roberta","last_name":"Schulte","first_name":"Roberta"},{"last_name":"Mair","full_name":"Mair, William","first_name":"William"},{"last_name":"Wagner","full_name":"Wagner, Ulrich","first_name":"Ulrich"},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","last_name":"HETZER"}],"scopus_import":"1","day":"05","publication_status":"published","publication_identifier":{"issn":["0092-8674"]},"intvolume":"       140","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"}],"month":"02","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","issue":"3","citation":{"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>","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.","short":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, M. Hetzer, Cell 140 (2010) 372–383.","chicago":"Capelson, Maya, Yun Liang, Roberta Schulte, William Mair, Ulrich Wagner, and Martin Hetzer. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression in Higher Eukaryotes.” <i>Cell</i>. Elsevier, 2010. <a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">https://doi.org/10.1016/j.cell.2009.12.054</a>.","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.","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>","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>."},"language":[{"iso":"eng"}],"oa":1},{"month":"11","oa":1,"language":[{"iso":"eng"}],"issue":"5","citation":{"ama":"Hetzer M, Wente SR. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. <i>Developmental Cell</i>. 2009;17(5):606-616. doi:<a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">10.1016/j.devcel.2009.10.007</a>","short":"M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.","ieee":"M. Hetzer and S. R. Wente, “Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes,” <i>Developmental Cell</i>, vol. 17, no. 5. Elsevier, pp. 606–616, 2009.","ista":"Hetzer M, Wente SR. 2009. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. Developmental Cell. 17(5), 606–616.","chicago":"Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis and Organization of the Nuclear Membrane and Pore Complexes.” <i>Developmental Cell</i>. Elsevier, 2009. <a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">https://doi.org/10.1016/j.devcel.2009.10.007</a>.","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>.","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>"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","author":[{"first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"},{"last_name":"Wente","full_name":"Wente, Susan R.","first_name":"Susan R."}],"scopus_import":"1","day":"17","oa_version":"Published Version","title":"Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes","volume":17,"article_type":"review","date_created":"2022-04-07T07:53:45Z","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"}],"intvolume":"        17","publication_identifier":{"issn":["1534-5807"]},"publication_status":"published","year":"2009","external_id":{"pmid":["19922866"]},"keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"status":"public","publication":"Developmental Cell","extern":"1","pmid":1,"date_published":"2009-11-17T00:00:00Z","doi":"10.1016/j.devcel.2009.10.007","article_processing_charge":"No","publisher":"Elsevier","date_updated":"2022-07-18T08:55:01Z","_id":"11103","type":"journal_article","page":"606-616","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2009.10.007"}],"quality_controlled":"1"},{"oa":1,"language":[{"iso":"eng"}],"citation":{"apa":"D’Angelo, M. A., Raices, M., Panowski, S. H., &#38; Hetzer, M. (2009). Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">https://doi.org/10.1016/j.cell.2008.11.037</a>","mla":"D’Angelo, Maximiliano A., et al. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” <i>Cell</i>, vol. 136, no. 2, Elsevier, 2009, pp. 284–95, doi:<a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">10.1016/j.cell.2008.11.037</a>.","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.","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.","short":"M.A. D’Angelo, M. Raices, S.H. Panowski, M. Hetzer, Cell 136 (2009) 284–295.","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>"},"issue":"2","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","month":"01","abstract":[{"text":"In dividing cells, nuclear pore complexes (NPCs) disassemble during mitosis and reassemble into the newly forming nuclei. However, the fate of nuclear pores in postmitotic cells is unknown. Here, we show that NPCs, unlike other nuclear structures, do not turn over in differentiated cells. While a subset of NPC components, like Nup153 and Nup50, are continuously exchanged, scaffold nucleoporins, like the Nup107/160 complex, are extremely long-lived and remain incorporated in the nuclear membrane during the entire cellular life span. Besides the lack of nucleoporin expression and NPC turnover, we discovered an age-related deterioration of NPCs, leading to an increase in nuclear permeability and the leaking of cytoplasmic proteins into the nucleus. Our finding that nuclear “leakiness” is dramatically accelerated during aging and that a subset of nucleoporins is oxidatively damaged in old cells suggests that the accumulation of damage at the NPC might be a crucial aging event.","lang":"eng"}],"intvolume":"       136","publication_identifier":{"issn":["0092-8674"]},"publication_status":"published","scopus_import":"1","day":"23","author":[{"first_name":"Maximiliano A.","full_name":"D'Angelo, Maximiliano A.","last_name":"D'Angelo"},{"first_name":"Marcela","full_name":"Raices, Marcela","last_name":"Raices"},{"last_name":"Panowski","full_name":"Panowski, Siler H.","first_name":"Siler H."},{"first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"}],"title":"Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells","oa_version":"Published Version","volume":136,"date_created":"2022-04-07T07:54:52Z","article_type":"original","publication":"Cell","extern":"1","status":"public","pmid":1,"date_published":"2009-01-23T00:00:00Z","year":"2009","external_id":{"pmid":["19167330"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"page":"284-295","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2008.11.037"}],"quality_controlled":"1","article_processing_charge":"No","doi":"10.1016/j.cell.2008.11.037","publisher":"Elsevier","_id":"11108","date_updated":"2022-07-18T08:55:29Z","type":"journal_article"}]