[{"date_updated":"2021-01-12T08:19:15Z","language":[{"iso":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","keyword":["General Biochemistry","Genetics and Molecular Biology"],"doi":"10.1016/j.cell.2018.10.039","publication_identifier":{"issn":["0092-8674"]},"day":"15","article_type":"original","oa_version":"None","year":"2018","type":"journal_article","author":[{"last_name":"Weinhäupl","full_name":"Weinhäupl, Katharina","first_name":"Katharina"},{"last_name":"Lindau","first_name":"Caroline","full_name":"Lindau, Caroline"},{"first_name":"Audrey","full_name":"Hessel, Audrey","last_name":"Hessel"},{"last_name":"Wang","full_name":"Wang, Yong","first_name":"Yong"},{"last_name":"Schütze","first_name":"Conny","full_name":"Schütze, Conny"},{"last_name":"Jores","full_name":"Jores, Tobias","first_name":"Tobias"},{"last_name":"Melchionda","first_name":"Laura","full_name":"Melchionda, Laura"},{"last_name":"Schönfisch","full_name":"Schönfisch, Birgit","first_name":"Birgit"},{"full_name":"Kalbacher, Hubert","first_name":"Hubert","last_name":"Kalbacher"},{"first_name":"Beate","full_name":"Bersch, Beate","last_name":"Bersch"},{"last_name":"Rapaport","full_name":"Rapaport, Doron","first_name":"Doron"},{"last_name":"Brennich","first_name":"Martha","full_name":"Brennich, Martha"},{"full_name":"Lindorff-Larsen, Kresten","first_name":"Kresten","last_name":"Lindorff-Larsen"},{"full_name":"Wiedemann, Nils","first_name":"Nils","last_name":"Wiedemann"},{"last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"}],"citation":{"chicago":"Weinhäupl, Katharina, Caroline Lindau, Audrey Hessel, Yong Wang, Conny Schütze, Tobias Jores, Laura Melchionda, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” <i>Cell</i>. Elsevier, 2018. <a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">https://doi.org/10.1016/j.cell.2018.10.039</a>.","ista":"Weinhäupl K, Lindau C, Hessel A, Wang Y, Schütze C, Jores T, Melchionda L, Schönfisch B, Kalbacher H, Bersch B, Rapaport D, Brennich M, Lindorff-Larsen K, Wiedemann N, Schanda P. 2018. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. 175(5), 1365–1379.e25.","ieee":"K. Weinhäupl <i>et al.</i>, “Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space,” <i>Cell</i>, vol. 175, no. 5. Elsevier, p. 1365–1379.e25, 2018.","mla":"Weinhäupl, Katharina, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” <i>Cell</i>, vol. 175, no. 5, Elsevier, 2018, p. 1365–1379.e25, doi:<a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">10.1016/j.cell.2018.10.039</a>.","short":"K. Weinhäupl, C. Lindau, A. Hessel, Y. Wang, C. Schütze, T. Jores, L. Melchionda, B. Schönfisch, H. Kalbacher, B. Bersch, D. Rapaport, M. Brennich, K. Lindorff-Larsen, N. Wiedemann, P. Schanda, Cell 175 (2018) 1365–1379.e25.","ama":"Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. <i>Cell</i>. 2018;175(5):1365-1379.e25. doi:<a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">10.1016/j.cell.2018.10.039</a>","apa":"Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., … Schanda, P. (2018). Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">https://doi.org/10.1016/j.cell.2018.10.039</a>"},"title":"Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space","quality_controlled":"1","publication":"Cell","volume":175,"intvolume":"       175","status":"public","publication_status":"published","publisher":"Elsevier","extern":"1","month":"11","_id":"8436","date_created":"2020-09-18T10:04:39Z","date_published":"2018-11-15T00:00:00Z","abstract":[{"text":"The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local binding events. Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial “transfer-chaperone” system is able to guide α-helical and β-barrel membrane proteins in a “nascent chain-like” conformation through a ribosome-free compartment.","lang":"eng"}],"page":"1365-1379.e25","issue":"5","article_processing_charge":"No"},{"article_processing_charge":"No","issue":"8","page":"2106-2113","_id":"8439","date_created":"2020-09-18T10:05:09Z","date_published":"2018-07-02T00:00:00Z","abstract":[{"lang":"eng","text":"Lipopolysaccharides (LPS) are complex glycolipids forming the outside layer of Gram-negative bacteria. Their hydrophobic and heterogeneous nature greatly hampers their structural study in an environment similar to the bacterial surface. We have studied LPS purified from E. coli and pathogenic P. aeruginosa with long O-antigen polysaccharides assembled in solution as vesicles or elongated micelles. Solid-state NMR with magic-angle spinning permitted the identification of NMR signals arising from regions with different flexibilities in the LPS, from the lipid components to the O-antigen polysaccharides. Atomic scale data on the LPS enabled the study of the interaction of gentamicin antibiotic bound to P. aeruginosa LPS, for which we could confirm that a specific oligosaccharide is involved in the antibiotic binding. The possibility to study LPS alone and bound to a ligand when it is assembled in membrane-like structures opens great prospects for the investigation of proteins and antibiotics that specifically target such an important molecule at the surface of Gram-negative bacteria."}],"month":"07","extern":"1","publisher":"American Chemical Society","publication_status":"published","status":"public","intvolume":"        13","volume":13,"publication":"ACS Chemical Biology","quality_controlled":"1","title":"Solid state NMR studies of intact lipopolysaccharide endotoxin","citation":{"chicago":"Laguri, Cedric, Alba Silipo, Alessandra M. Martorana, Paul Schanda, Roberta Marchetti, Alessandra Polissi, Antonio Molinaro, and Jean-Pierre Simorre. “Solid State NMR Studies of Intact Lipopolysaccharide Endotoxin.” <i>ACS Chemical Biology</i>. American Chemical Society, 2018. <a href=\"https://doi.org/10.1021/acschembio.8b00271\">https://doi.org/10.1021/acschembio.8b00271</a>.","ieee":"C. Laguri <i>et al.</i>, “Solid state NMR studies of intact lipopolysaccharide endotoxin,” <i>ACS Chemical Biology</i>, vol. 13, no. 8. American Chemical Society, pp. 2106–2113, 2018.","ista":"Laguri C, Silipo A, Martorana AM, Schanda P, Marchetti R, Polissi A, Molinaro A, Simorre J-P. 2018. Solid state NMR studies of intact lipopolysaccharide endotoxin. ACS Chemical Biology. 13(8), 2106–2113.","mla":"Laguri, Cedric, et al. “Solid State NMR Studies of Intact Lipopolysaccharide Endotoxin.” <i>ACS Chemical Biology</i>, vol. 13, no. 8, American Chemical Society, 2018, pp. 2106–13, doi:<a href=\"https://doi.org/10.1021/acschembio.8b00271\">10.1021/acschembio.8b00271</a>.","short":"C. Laguri, A. Silipo, A.M. Martorana, P. Schanda, R. Marchetti, A. Polissi, A. Molinaro, J.-P. Simorre, ACS Chemical Biology 13 (2018) 2106–2113.","ama":"Laguri C, Silipo A, Martorana AM, et al. Solid state NMR studies of intact lipopolysaccharide endotoxin. <i>ACS Chemical Biology</i>. 2018;13(8):2106-2113. doi:<a href=\"https://doi.org/10.1021/acschembio.8b00271\">10.1021/acschembio.8b00271</a>","apa":"Laguri, C., Silipo, A., Martorana, A. M., Schanda, P., Marchetti, R., Polissi, A., … Simorre, J.-P. (2018). Solid state NMR studies of intact lipopolysaccharide endotoxin. <i>ACS Chemical Biology</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acschembio.8b00271\">https://doi.org/10.1021/acschembio.8b00271</a>"},"type":"journal_article","author":[{"last_name":"Laguri","first_name":"Cedric","full_name":"Laguri, Cedric"},{"full_name":"Silipo, Alba","first_name":"Alba","last_name":"Silipo"},{"last_name":"Martorana","full_name":"Martorana, Alessandra M.","first_name":"Alessandra M."},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda"},{"last_name":"Marchetti","full_name":"Marchetti, Roberta","first_name":"Roberta"},{"first_name":"Alessandra","full_name":"Polissi, Alessandra","last_name":"Polissi"},{"last_name":"Molinaro","full_name":"Molinaro, Antonio","first_name":"Antonio"},{"last_name":"Simorre","first_name":"Jean-Pierre","full_name":"Simorre, Jean-Pierre"}],"year":"2018","oa_version":"None","article_type":"original","day":"02","publication_identifier":{"issn":["1554-8929","1554-8937"]},"doi":"10.1021/acschembio.8b00271","keyword":["Molecular Medicine","Biochemistry","General Medicine"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","language":[{"iso":"eng"}],"date_updated":"2021-01-12T08:19:16Z"},{"page":"8379-8393","article_processing_charge":"No","issue":"22","month":"06","extern":"1","abstract":[{"lang":"eng","text":"Mycobacterium tuberculosis can remain dormant in the host, an ability that explains the failure of many current tuberculosis treatments. Recently, the natural products cyclomarin, ecumicin, and lassomycin have been shown to efficiently kill Mycobacterium tuberculosis persisters. Their target is the N-terminal domain of the hexameric AAA+ ATPase ClpC1, which recognizes, unfolds, and translocates protein substrates, such as proteins containing phosphorylated arginine residues, to the ClpP1P2 protease for degradation. Surprisingly, these antibiotics do not inhibit ClpC1 ATPase activity, and how they cause cell death is still unclear. Here, using NMR and small-angle X-ray scattering, we demonstrate that arginine-phosphate binding to the ClpC1 N-terminal domain induces millisecond dynamics. We show that these dynamics are caused by conformational changes and do not result from unfolding or oligomerization of this domain. Cyclomarin binding to this domain specifically blocked these N-terminal dynamics. On the basis of these results, we propose a mechanism of action involving cyclomarin-induced restriction of ClpC1 dynamics, which modulates the chaperone enzymatic activity leading eventually to cell death."}],"_id":"8440","date_created":"2020-09-18T10:05:18Z","date_published":"2018-06-01T00:00:00Z","publication_status":"published","publisher":"American Society for Biochemistry & Molecular Biology","publication":"Journal of Biological Chemistry","quality_controlled":"1","status":"public","intvolume":"       293","volume":293,"citation":{"short":"K. Weinhäupl, M. Brennich, U. Kazmaier, J. Lelievre, L. Ballell, A. Goldberg, P. Schanda, H. Fraga, Journal of Biological Chemistry 293 (2018) 8379–8393.","apa":"Weinhäupl, K., Brennich, M., Kazmaier, U., Lelievre, J., Ballell, L., Goldberg, A., … Fraga, H. (2018). The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology. <a href=\"https://doi.org/10.1074/jbc.ra118.002251\">https://doi.org/10.1074/jbc.ra118.002251</a>","ama":"Weinhäupl K, Brennich M, Kazmaier U, et al. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. <i>Journal of Biological Chemistry</i>. 2018;293(22):8379-8393. doi:<a href=\"https://doi.org/10.1074/jbc.ra118.002251\">10.1074/jbc.ra118.002251</a>","ista":"Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda P, Fraga H. 2018. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. 293(22), 8379–8393.","ieee":"K. Weinhäupl <i>et al.</i>, “The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis,” <i>Journal of Biological Chemistry</i>, vol. 293, no. 22. American Society for Biochemistry &#38; Molecular Biology, pp. 8379–8393, 2018.","chicago":"Weinhäupl, Katharina, Martha Brennich, Uli Kazmaier, Joel Lelievre, Lluis Ballell, Alfred Goldberg, Paul Schanda, and Hugo Fraga. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology, 2018. <a href=\"https://doi.org/10.1074/jbc.ra118.002251\">https://doi.org/10.1074/jbc.ra118.002251</a>.","mla":"Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” <i>Journal of Biological Chemistry</i>, vol. 293, no. 22, American Society for Biochemistry &#38; Molecular Biology, 2018, pp. 8379–93, doi:<a href=\"https://doi.org/10.1074/jbc.ra118.002251\">10.1074/jbc.ra118.002251</a>."},"title":"The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis","article_type":"original","day":"01","type":"journal_article","author":[{"last_name":"Weinhäupl","first_name":"Katharina","full_name":"Weinhäupl, Katharina"},{"last_name":"Brennich","full_name":"Brennich, Martha","first_name":"Martha"},{"first_name":"Uli","full_name":"Kazmaier, Uli","last_name":"Kazmaier"},{"last_name":"Lelievre","first_name":"Joel","full_name":"Lelievre, Joel"},{"last_name":"Ballell","full_name":"Ballell, Lluis","first_name":"Lluis"},{"full_name":"Goldberg, Alfred","first_name":"Alfred","last_name":"Goldberg"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda"},{"last_name":"Fraga","full_name":"Fraga, Hugo","first_name":"Hugo"}],"year":"2018","oa_version":"None","keyword":["Cell Biology","Biochemistry","Molecular Biology"],"language":[{"iso":"eng"}],"date_updated":"2021-01-12T08:19:17Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["0021-9258","1083-351X"]},"doi":"10.1074/jbc.ra118.002251"},{"extern":"1","month":"02","date_created":"2023-08-01T09:39:32Z","publisher":"Springer Nature","quality_controlled":"1","publication":"Nature Communications","intvolume":"         9","status":"public","citation":{"ista":"Samanta D, Galaktionova D, Gemen J, Shimon LJW, Diskin-Posner Y, Avram L, Král P, Klajn R. 2018. Reversible chromism of spiropyran in the cavity of a flexible coordination cage. Nature Communications. 9, 641.","ieee":"D. Samanta <i>et al.</i>, “Reversible chromism of spiropyran in the cavity of a flexible coordination cage,” <i>Nature Communications</i>, vol. 9. Springer Nature, 2018.","chicago":"Samanta, Dipak, Daria Galaktionova, Julius Gemen, Linda J. W. Shimon, Yael Diskin-Posner, Liat Avram, Petr Král, and Rafal Klajn. “Reversible Chromism of Spiropyran in the Cavity of a Flexible Coordination Cage.” <i>Nature Communications</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41467-017-02715-6\">https://doi.org/10.1038/s41467-017-02715-6</a>.","mla":"Samanta, Dipak, et al. “Reversible Chromism of Spiropyran in the Cavity of a Flexible Coordination Cage.” <i>Nature Communications</i>, vol. 9, 641, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41467-017-02715-6\">10.1038/s41467-017-02715-6</a>.","short":"D. Samanta, D. Galaktionova, J. Gemen, L.J.W. Shimon, Y. Diskin-Posner, L. Avram, P. Král, R. Klajn, Nature Communications 9 (2018).","apa":"Samanta, D., Galaktionova, D., Gemen, J., Shimon, L. J. W., Diskin-Posner, Y., Avram, L., … Klajn, R. (2018). Reversible chromism of spiropyran in the cavity of a flexible coordination cage. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-017-02715-6\">https://doi.org/10.1038/s41467-017-02715-6</a>","ama":"Samanta D, Galaktionova D, Gemen J, et al. Reversible chromism of spiropyran in the cavity of a flexible coordination cage. <i>Nature Communications</i>. 2018;9. doi:<a href=\"https://doi.org/10.1038/s41467-017-02715-6\">10.1038/s41467-017-02715-6</a>"},"title":"Reversible chromism of spiropyran in the cavity of a flexible coordination cage","day":"13","type":"journal_article","author":[{"first_name":"Dipak","full_name":"Samanta, Dipak","last_name":"Samanta"},{"full_name":"Galaktionova, Daria","first_name":"Daria","last_name":"Galaktionova"},{"full_name":"Gemen, Julius","first_name":"Julius","last_name":"Gemen"},{"first_name":"Linda J. W.","full_name":"Shimon, Linda J. W.","last_name":"Shimon"},{"full_name":"Diskin-Posner, Yael","first_name":"Yael","last_name":"Diskin-Posner"},{"last_name":"Avram","full_name":"Avram, Liat","first_name":"Liat"},{"last_name":"Král","first_name":"Petr","full_name":"Král, Petr"},{"id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn","full_name":"Klajn, Rafal","first_name":"Rafal"}],"pmid":1,"related_material":{"link":[{"url":"https://doi.org/10.1038/s41467-018-03701-2","relation":"erratum"}]},"language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"doi":"10.1038/s41467-017-02715-6","article_processing_charge":"No","article_number":"641","_id":"13374","date_published":"2018-02-13T00:00:00Z","abstract":[{"lang":"eng","text":"Confining molecules to volumes only slightly larger than the molecules themselves can profoundly alter their properties. Molecular switches—entities that can be toggled between two or more forms upon exposure to an external stimulus—often require conformational freedom to isomerize. Therefore, placing these switches in confined spaces can render them non-operational. To preserve the switchability of these species under confinement, we work with a water-soluble coordination cage that is flexible enough to adapt its shape to the conformation of the encapsulated guest. We show that owing to its flexibility, the cage is not only capable of accommodating—and solubilizing in water—several light-responsive spiropyran-based molecular switches, but, more importantly, it also provides an environment suitable for the efficient, reversible photoisomerization of the bound guests. Our findings pave the way towards studying various molecular switching processes in confined environments."}],"publication_status":"published","oa":1,"main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-02715-6","open_access":"1"}],"volume":9,"article_type":"original","year":"2018","oa_version":"Published Version","date_updated":"2023-08-07T10:54:05Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":"1","external_id":{"pmid":["29440687"]},"publication_identifier":{"eissn":["2041-1723"]}},{"quality_controlled":"1","publication":"Nature Communications","intvolume":"         9","status":"public","publisher":"Springer Nature","extern":"1","month":"05","date_created":"2023-09-06T12:07:33Z","language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"doi":"10.1038/s41467-018-04139-2","pmid":1,"day":"04","author":[{"full_name":"Bräuning, Bastian","first_name":"Bastian","last_name":"Bräuning"},{"full_name":"Bertosin, Eva","first_name":"Eva","last_name":"Bertosin"},{"last_name":"Praetorius","full_name":"Praetorius, Florian M","first_name":"Florian M","id":"dfec9381-4341-11ee-8fd8-faa02bba7d62"},{"last_name":"Ihling","first_name":"Christian","full_name":"Ihling, Christian"},{"full_name":"Schatt, Alexandra","first_name":"Alexandra","last_name":"Schatt"},{"full_name":"Adler, Agnes","first_name":"Agnes","last_name":"Adler"},{"first_name":"Klaus","full_name":"Richter, Klaus","last_name":"Richter"},{"full_name":"Sinz, Andrea","first_name":"Andrea","last_name":"Sinz"},{"last_name":"Dietz","full_name":"Dietz, Hendrik","first_name":"Hendrik"},{"full_name":"Groll, Michael","first_name":"Michael","last_name":"Groll"}],"type":"journal_article","citation":{"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>.","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.","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.","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>.","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)."},"title":"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB","volume":9,"publication_status":"published","main_file_link":[{"url":"https://doi.org/10.1038/s41467-018-04139-2","open_access":"1"}],"oa":1,"article_number":"1806","date_published":"2018-05-04T00:00:00Z","_id":"14284","abstract":[{"lang":"eng","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."}],"article_processing_charge":"No","date_updated":"2023-11-07T11:46:12Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"pmid":["29728606"]},"scopus_import":"1","publication_identifier":{"issn":["2041-1723"]},"article_type":"original","oa_version":"Published Version","year":"2018"},{"publisher":"Springer Nature","publication":"Nature Communications","quality_controlled":"1","intvolume":"         8","status":"public","month":"08","extern":"1","date_created":"2022-04-07T07:45:50Z","pmid":1,"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"language":[{"iso":"eng"}],"doi":"10.1038/s41467-017-00322-z","citation":{"ista":"Buchwalter A, Hetzer M. 2017. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 8, 328.","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>.","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>.","short":"A. Buchwalter, M. Hetzer, Nature Communications 8 (2017).","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>","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>"},"title":"Nucleolar expansion and elevated protein translation in premature aging","day":"30","author":[{"last_name":"Buchwalter","first_name":"Abigail","full_name":"Buchwalter, Abigail"},{"first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"}],"type":"journal_article","publication_status":"published","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-017-00322-z"}],"oa":1,"volume":8,"article_processing_charge":"No","article_number":"328","_id":"11065","date_published":"2017-08-30T00:00:00Z","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."}],"external_id":{"pmid":["28855503"]},"scopus_import":"1","date_updated":"2022-07-18T08:33:03Z","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publication_identifier":{"issn":["2041-1723"]},"article_type":"original","oa_version":"Published Version","year":"2017"},{"page":"125-129","article_processing_charge":"No","issue":"8","month":"08","extern":"1","_id":"8448","date_published":"2017-08-01T00:00:00Z","date_created":"2020-09-18T10:06:27Z","abstract":[{"lang":"eng","text":"We present an improved fast mixing device based on the rapid mixing of two solutions inside the NMR probe, as originally proposed by Hore and coworkers (J. Am. Chem. Soc. 125 (2003) 12484–12492). Such a device is important for off-equilibrium studies of molecular kinetics by multidimensional real-time NMR spectrsocopy. The novelty of this device is that it allows removing the injector from the NMR detection volume after mixing, and thus provides good magnetic field homogeneity independently of the initial sample volume placed in the NMR probe. The apparatus is simple to build, inexpensive, and can be used without any hardware modification on any type of liquid-state NMR spectrometer. We demonstrate the performance of our fast mixing device in terms of improved magnetic field homogeneity, and show an application to the study of protein folding and the structural characterization of transiently populated folding intermediates."}],"publication_status":"published","publisher":"Elsevier","publication":"Journal of Magnetic Resonance","quality_controlled":"1","intvolume":"       281","status":"public","volume":281,"citation":{"mla":"Franco, Rémi, et al. “Optimized Fast Mixing Device for Real-Time NMR Applications.” <i>Journal of Magnetic Resonance</i>, vol. 281, no. 8, Elsevier, 2017, pp. 125–29, doi:<a href=\"https://doi.org/10.1016/j.jmr.2017.05.016\">10.1016/j.jmr.2017.05.016</a>.","ista":"Franco R, Favier A, Schanda P, Brutscher B. 2017. Optimized fast mixing device for real-time NMR applications. Journal of Magnetic Resonance. 281(8), 125–129.","ieee":"R. Franco, A. Favier, P. Schanda, and B. Brutscher, “Optimized fast mixing device for real-time NMR applications,” <i>Journal of Magnetic Resonance</i>, vol. 281, no. 8. Elsevier, pp. 125–129, 2017.","chicago":"Franco, Rémi, Adrien Favier, Paul Schanda, and Bernhard Brutscher. “Optimized Fast Mixing Device for Real-Time NMR Applications.” <i>Journal of Magnetic Resonance</i>. Elsevier, 2017. <a href=\"https://doi.org/10.1016/j.jmr.2017.05.016\">https://doi.org/10.1016/j.jmr.2017.05.016</a>.","apa":"Franco, R., Favier, A., Schanda, P., &#38; Brutscher, B. (2017). Optimized fast mixing device for real-time NMR applications. <i>Journal of Magnetic Resonance</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmr.2017.05.016\">https://doi.org/10.1016/j.jmr.2017.05.016</a>","ama":"Franco R, Favier A, Schanda P, Brutscher B. Optimized fast mixing device for real-time NMR applications. <i>Journal of Magnetic Resonance</i>. 2017;281(8):125-129. doi:<a href=\"https://doi.org/10.1016/j.jmr.2017.05.016\">10.1016/j.jmr.2017.05.016</a>","short":"R. Franco, A. Favier, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 281 (2017) 125–129."},"title":"Optimized fast mixing device for real-time NMR applications","article_type":"original","day":"01","author":[{"first_name":"Rémi","full_name":"Franco, Rémi","last_name":"Franco"},{"first_name":"Adrien","full_name":"Favier, Adrien","last_name":"Favier"},{"first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"}],"type":"journal_article","oa_version":"None","year":"2017","keyword":["Nuclear and High Energy Physics","Biophysics","Biochemistry","Condensed Matter Physics"],"language":[{"iso":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2021-01-12T08:19:20Z","publication_identifier":{"issn":["1090-7807"]},"doi":"10.1016/j.jmr.2017.05.016"},{"publication_status":"published","volume":139,"issue":"49","article_processing_charge":"No","_id":"13380","date_published":"2017-12-01T00:00:00Z","abstract":[{"text":"Although dissipative self-assembly is ubiquitous in nature, where it gives rise to structures and functions critical to life, examples of artificial systems featuring this mode of self-assembly are rare. Here, we identify the presence of ephemeral assemblies during seeded growth of gold nanoparticles. In this process, hydrazine reduces Au(III) ions, which attach to the existing nanoparticles “seeds”. The attachment is accompanied by a local increase in the concentration of a surfactant, which therefore forms a bilayer on nanoparticle surfaces, inducing their assembly. The resulting aggregates gradually disassemble as the surfactant concentration throughout the solution equilibrates. The lifetimes of the out-of-equilibrium aggregates depend on and can be controlled by the size of the constituent nanoparticles. We demonstrate the utility of our out-of-equilibrium aggregates to form transient reflective coatings on polar surfaces.","lang":"eng"}],"publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2023-08-07T11:19:30Z","external_id":{"pmid":["29193964"]},"scopus_import":"1","oa_version":"None","year":"2017","article_type":"original","publisher":"American Chemical Society","status":"public","intvolume":"       139","quality_controlled":"1","publication":"Journal of the American Chemical Society","page":"17973-17978","date_created":"2023-08-01T09:41:01Z","extern":"1","month":"12","pmid":1,"doi":"10.1021/jacs.7b09111","language":[{"iso":"eng"}],"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"title":"Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles","citation":{"chicago":"Sawczyk, Michał, and Rafal Klajn. “Out-of-Equilibrium Aggregates and Coatings during Seeded Growth of Metallic Nanoparticles.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2017. <a href=\"https://doi.org/10.1021/jacs.7b09111\">https://doi.org/10.1021/jacs.7b09111</a>.","ista":"Sawczyk M, Klajn R. 2017. Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles. Journal of the American Chemical Society. 139(49), 17973–17978.","ieee":"M. Sawczyk and R. Klajn, “Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles,” <i>Journal of the American Chemical Society</i>, vol. 139, no. 49. American Chemical Society, pp. 17973–17978, 2017.","mla":"Sawczyk, Michał, and Rafal Klajn. “Out-of-Equilibrium Aggregates and Coatings during Seeded Growth of Metallic Nanoparticles.” <i>Journal of the American Chemical Society</i>, vol. 139, no. 49, American Chemical Society, 2017, pp. 17973–78, doi:<a href=\"https://doi.org/10.1021/jacs.7b09111\">10.1021/jacs.7b09111</a>.","short":"M. Sawczyk, R. Klajn, Journal of the American Chemical Society 139 (2017) 17973–17978.","ama":"Sawczyk M, Klajn R. Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles. <i>Journal of the American Chemical Society</i>. 2017;139(49):17973-17978. doi:<a href=\"https://doi.org/10.1021/jacs.7b09111\">10.1021/jacs.7b09111</a>","apa":"Sawczyk, M., &#38; Klajn, R. (2017). Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jacs.7b09111\">https://doi.org/10.1021/jacs.7b09111</a>"},"author":[{"full_name":"Sawczyk, Michał","first_name":"Michał","last_name":"Sawczyk"},{"last_name":"Klajn","full_name":"Klajn, Rafal","first_name":"Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"type":"journal_article","day":"01"},{"article_number":"15651","abstract":[{"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.","lang":"eng"}],"_id":"14005","date_published":"2017-06-15T00:00:00Z","article_processing_charge":"No","volume":8,"publication_status":"published","oa":1,"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms15651"}],"article_type":"original","year":"2017","oa_version":"Published Version","external_id":{"pmid":["28643771"]},"scopus_import":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2023-08-22T08:26:06Z","publication_identifier":{"eissn":["2041-1723"]},"month":"06","extern":"1","date_created":"2023-08-10T06:36:09Z","publication":"Nature Communications","quality_controlled":"1","intvolume":"         8","status":"public","publisher":"Springer Nature","day":"15","author":[{"last_name":"Walt","first_name":"Samuel G.","full_name":"Walt, Samuel G."},{"first_name":"Niraghatam","full_name":"Bhargava Ram, Niraghatam","last_name":"Bhargava Ram"},{"first_name":"Marcos","full_name":"Atala, Marcos","last_name":"Atala"},{"full_name":"Shvetsov-Shilovski, Nikolay I","first_name":"Nikolay I","last_name":"Shvetsov-Shilovski"},{"first_name":"Aaron","full_name":"von Conta, Aaron","last_name":"von Conta"},{"id":"71b4d059-2a03-11ee-914d-dfa3beed6530","first_name":"Denitsa Rangelova","full_name":"Baykusheva, Denitsa Rangelova","last_name":"Baykusheva"},{"first_name":"Manfred","full_name":"Lein, Manfred","last_name":"Lein"},{"last_name":"Wörner","full_name":"Wörner, Hans Jakob","first_name":"Hans Jakob"}],"type":"journal_article","citation":{"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>","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>","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).","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>.","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.","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."},"title":"Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"language":[{"iso":"eng"}],"doi":"10.1038/ncomms15651","pmid":1},{"day":"09","author":[{"last_name":"Helle","full_name":"Helle, Sebastian Carsten Johannes","first_name":"Sebastian Carsten Johannes"},{"first_name":"Qian","full_name":"Feng, Qian","last_name":"Feng"},{"first_name":"Mathias J","full_name":"Aebersold, Mathias J","last_name":"Aebersold"},{"first_name":"Luca","full_name":"Hirt, Luca","last_name":"Hirt"},{"full_name":"Grüter, Raphael R","first_name":"Raphael R","last_name":"Grüter"},{"first_name":"Afshin","full_name":"Vahid, Afshin","last_name":"Vahid"},{"first_name":"Andrea","full_name":"Sirianni, Andrea","last_name":"Sirianni"},{"last_name":"Mostowy","full_name":"Mostowy, Serge","first_name":"Serge"},{"last_name":"Snedeker","full_name":"Snedeker, Jess G","first_name":"Jess G"},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","orcid":"0000-0002-7854-2139","last_name":"Šarić","full_name":"Šarić, Anđela","first_name":"Anđela"},{"last_name":"Idema","full_name":"Idema, Timon","first_name":"Timon"},{"first_name":"Tomaso","full_name":"Zambelli, Tomaso","last_name":"Zambelli"},{"full_name":"Kornmann, Benoît","first_name":"Benoît","last_name":"Kornmann"}],"type":"journal_article","citation":{"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).","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>","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.","ieee":"S. C. J. Helle <i>et al.</i>, “Mechanical force induces mitochondrial fission,” <i>eLife</i>, vol. 6. eLife Sciences Publications, 2017.","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>."},"title":"Mechanical force induces mitochondrial fission","language":[{"iso":"eng"}],"keyword":["general immunology and microbiology","general biochemistry","genetics and molecular biology","general medicine","general neuroscience"],"doi":"10.7554/elife.30292","ddc":["572"],"pmid":1,"extern":"1","month":"11","date_created":"2021-11-29T08:51:38Z","quality_controlled":"1","publication":"eLife","status":"public","intvolume":"         6","publisher":"eLife Sciences Publications","article_type":"original","has_accepted_license":"1","year":"2017","oa_version":"Published Version","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","date_updated":"2021-11-29T09:28:14Z","scopus_import":"1","external_id":{"pmid":["29119945"]},"publication_identifier":{"issn":["2050-084X"]},"file":[{"content_type":"application/pdf","relation":"main_file","file_id":"10372","success":1,"date_created":"2021-11-29T09:07:41Z","file_name":"2017_eLife_Helle.pdf","file_size":6120157,"creator":"cchlebak","date_updated":"2021-11-29T09:07:41Z","access_level":"open_access","checksum":"c35f42dcfb007f6d6c761a27e24c26d3"}],"article_number":"e30292","abstract":[{"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.","lang":"eng"}],"_id":"10370","date_published":"2017-11-09T00:00:00Z","article_processing_charge":"No","file_date_updated":"2021-11-29T09:07:41Z","volume":6,"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)"},"publication_status":"published","main_file_link":[{"open_access":"1","url":"https://elifesciences.org/articles/30292"}],"oa":1},{"status":"public","intvolume":"         7","quality_controlled":"1","publication":"Nature Communications","publisher":"Springer Nature","date_created":"2022-04-07T07:48:34Z","extern":"1","month":"12","doi":"10.1038/ncomms13874","language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"pmid":1,"related_material":{"link":[{"url":"https://doi.org/10.1038/ncomms16030","relation":"erratum"}]},"author":[{"first_name":"Robert A.H.","full_name":"van de Ven, Robert A.H.","last_name":"van de Ven"},{"full_name":"de Groot, Jolien S.","first_name":"Jolien S.","last_name":"de Groot"},{"full_name":"Park, Danielle","first_name":"Danielle","last_name":"Park"},{"full_name":"van Domselaar, Robert","first_name":"Robert","last_name":"van Domselaar"},{"last_name":"de Jong","full_name":"de Jong, Danielle","first_name":"Danielle"},{"full_name":"Szuhai, Karoly","first_name":"Karoly","last_name":"Szuhai"},{"last_name":"van der Wall","full_name":"van der Wall, Elsken","first_name":"Elsken"},{"last_name":"Rueda","first_name":"Oscar M.","full_name":"Rueda, Oscar M."},{"last_name":"Ali","first_name":"H. Raza","full_name":"Ali, H. Raza"},{"first_name":"Carlos","full_name":"Caldas, Carlos","last_name":"Caldas"},{"last_name":"van Diest","full_name":"van Diest, Paul J.","first_name":"Paul J."},{"first_name":"Martin W","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"},{"full_name":"Sahai, Erik","first_name":"Erik","last_name":"Sahai"},{"full_name":"Derksen, Patrick W.B.","first_name":"Patrick W.B.","last_name":"Derksen"}],"type":"journal_article","day":"22","title":"p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis","citation":{"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>.","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.","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.","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>.","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>","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>","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)."},"volume":7,"oa":1,"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms13874"}],"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"}],"_id":"11072","date_published":"2016-12-22T00:00:00Z","article_number":"13874","article_processing_charge":"No","publication_identifier":{"issn":["2041-1723"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","date_updated":"2022-07-18T08:34:32Z","external_id":{"pmid":["28004812"]},"scopus_import":"1","oa_version":"Published Version","year":"2016","article_type":"original"},{"intvolume":"       161","status":"public","publication":"Cell","quality_controlled":"1","publisher":"Elsevier","date_created":"2022-04-07T07:48:49Z","month":"06","extern":"1","page":"1502-1504","doi":"10.1016/j.cell.2015.06.005","keyword":["General Biochemistry","Genetics and Molecular Biology"],"language":[{"iso":"eng"}],"pmid":1,"author":[{"last_name":"Hatch","first_name":"Emily M.","full_name":"Hatch, Emily M."},{"last_name":"HETZER","full_name":"HETZER, Martin W","first_name":"Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"type":"journal_article","day":"18","title":"Linking micronuclei to chromosome fragmentation","citation":{"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>","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>","short":"E.M. Hatch, M. Hetzer, Cell 161 (2015) 1502–1504.","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>.","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>.","ista":"Hatch EM, Hetzer M. 2015. Linking micronuclei to chromosome fragmentation. Cell. 161(7), 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."},"volume":161,"oa":1,"main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2015.06.005","open_access":"1"}],"publication_status":"published","_id":"11073","date_published":"2015-06-18T00:00:00Z","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."}],"article_processing_charge":"No","issue":"7","publication_identifier":{"issn":["0092-8674"]},"scopus_import":"1","external_id":{"pmid":["26091034"]},"date_updated":"2022-07-18T08:34:33Z","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa_version":"Published Version","year":"2015","article_type":"original"},{"volume":25,"publication_status":"published","main_file_link":[{"url":"https://doi.org/10.1016/j.cub.2015.02.033","open_access":"1"}],"oa":1,"_id":"11074","date_published":"2015-05-18T00:00:00Z","issue":"10","article_processing_charge":"No","date_updated":"2022-07-18T08:34:34Z","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","external_id":{"pmid":["25989073"]},"scopus_import":"1","publication_identifier":{"issn":["0960-9822"]},"article_type":"original","oa_version":"Published Version","year":"2015","quality_controlled":"1","publication":"Current Biology","status":"public","intvolume":"        25","publisher":"Elsevier","extern":"1","month":"05","date_created":"2022-04-07T07:49:00Z","page":"PR397-R399","language":[{"iso":"eng"}],"keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"doi":"10.1016/j.cub.2015.02.033","pmid":1,"day":"18","type":"journal_article","author":[{"last_name":"Hatch","full_name":"Hatch, Emily M.","first_name":"Emily M."},{"last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"citation":{"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>.","ista":"Hatch EM, Hetzer M. 2015. Chromothripsis. Current Biology. 25(10), PR397-R399.","ieee":"E. M. Hatch and M. Hetzer, “Chromothripsis,” <i>Current Biology</i>, vol. 25, no. 10. Elsevier, pp. PR397-R399, 2015.","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>.","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>","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>","short":"E.M. Hatch, M. Hetzer, Current Biology 25 (2015) PR397-R399."},"title":"Chromothripsis"},{"citation":{"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>.","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.","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.","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>.","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>","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>","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)."},"title":"Observing the overall rocking motion of a protein in a crystal","article_type":"original","day":"05","author":[{"last_name":"Ma","first_name":"Peixiang","full_name":"Ma, Peixiang"},{"full_name":"Xue, Yi","first_name":"Yi","last_name":"Xue"},{"last_name":"Coquelle","first_name":"Nicolas","full_name":"Coquelle, Nicolas"},{"last_name":"Haller","full_name":"Haller, Jens D.","first_name":"Jens D."},{"first_name":"Tairan","full_name":"Yuwen, Tairan","last_name":"Yuwen"},{"full_name":"Ayala, Isabel","first_name":"Isabel","last_name":"Ayala"},{"last_name":"Mikhailovskii","first_name":"Oleg","full_name":"Mikhailovskii, Oleg"},{"last_name":"Willbold","full_name":"Willbold, Dieter","first_name":"Dieter"},{"full_name":"Colletier, Jacques-Philippe","first_name":"Jacques-Philippe","last_name":"Colletier"},{"first_name":"Nikolai R.","full_name":"Skrynnikov, Nikolai R.","last_name":"Skrynnikov"},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda"}],"type":"journal_article","year":"2015","oa_version":"Published Version","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2021-01-12T08:19:24Z","language":[{"iso":"eng"}],"publication_identifier":{"issn":["2041-1723"]},"doi":"10.1038/ncomms9361","article_processing_charge":"No","month":"10","article_number":"8361","extern":"1","abstract":[{"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.","lang":"eng"}],"_id":"8456","date_created":"2020-09-18T10:07:36Z","date_published":"2015-10-05T00:00:00Z","publisher":"Springer Nature","publication_status":"published","publication":"Nature Communications","quality_controlled":"1","status":"public","intvolume":"         6","volume":6},{"day":"05","type":"journal_article","author":[{"last_name":"Kraus","full_name":"Kraus, P. M.","first_name":"P. M."},{"full_name":"Tolstikhin, O. I.","first_name":"O. I.","last_name":"Tolstikhin"},{"full_name":"Baykusheva, Denitsa Rangelova","first_name":"Denitsa Rangelova","last_name":"Baykusheva","id":"71b4d059-2a03-11ee-914d-dfa3beed6530"},{"last_name":"Rupenyan","full_name":"Rupenyan, A.","first_name":"A."},{"last_name":"Schneider","full_name":"Schneider, J.","first_name":"J."},{"full_name":"Bisgaard, C. Z.","first_name":"C. Z.","last_name":"Bisgaard"},{"first_name":"T.","full_name":"Morishita, T.","last_name":"Morishita"},{"first_name":"F.","full_name":"Jensen, F.","last_name":"Jensen"},{"full_name":"Madsen, L. B.","first_name":"L. B.","last_name":"Madsen"},{"first_name":"H. J.","full_name":"Wörner, H. J.","last_name":"Wörner"}],"citation":{"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).","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>","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>","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.","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.","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>."},"title":"Observation of laser-induced electronic structure in oriented polyatomic molecules","language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"doi":"10.1038/ncomms8039","pmid":1,"extern":"1","month":"05","date_created":"2023-08-10T06:38:01Z","quality_controlled":"1","publication":"Nature Communications","intvolume":"         6","status":"public","publisher":"Springer Nature","article_type":"original","year":"2015","oa_version":"Published Version","date_updated":"2023-08-22T08:52:56Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":"1","external_id":{"pmid":["25940229"]},"publication_identifier":{"eissn":["2041-1723"]},"article_number":"7039","abstract":[{"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.","lang":"eng"}],"_id":"14016","date_published":"2015-05-05T00:00:00Z","article_processing_charge":"No","volume":6,"publication_status":"published","main_file_link":[{"url":"https://doi.org/10.1038/ncomms8039","open_access":"1"}],"oa":1},{"date_updated":"2022-07-18T08:44:33Z","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","scopus_import":"1","external_id":{"pmid":["24581486"]},"publication_identifier":{"issn":["0092-8674"]},"article_type":"original","year":"2014","oa_version":"Published Version","volume":156,"publication_status":"published","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2014.02.004"}],"oa":1,"date_published":"2014-02-27T00:00:00Z","_id":"11080","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"}],"issue":"5","article_processing_charge":"No","language":[{"iso":"eng"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"doi":"10.1016/j.cell.2014.02.004","pmid":1,"day":"27","type":"journal_article","author":[{"first_name":"Abigail","full_name":"Buchwalter, Abigail","last_name":"Buchwalter"},{"orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"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>.","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>.","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.","ista":"Buchwalter A, Hetzer M. 2014. Nuclear pores set the speed limit for mitosis. Cell. 156(5), 868–869.","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>","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>","short":"A. Buchwalter, M. Hetzer, Cell 156 (2014) 868–869."},"title":"Nuclear pores set the speed limit for mitosis","quality_controlled":"1","publication":"Cell","intvolume":"       156","status":"public","publisher":"Elsevier","extern":"1","month":"02","date_created":"2022-04-07T07:50:04Z","page":"868-869"},{"oa_version":"None","year":"2014","article_type":"original","publication_identifier":{"issn":["1367-4803","1460-2059"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2021-01-12T08:19:25Z","issue":"15","article_processing_charge":"No","date_published":"2014-08-01T00:00:00Z","_id":"8459","abstract":[{"text":"Nuclear magnetic resonance (NMR) is a powerful tool for observing the motion of biomolecules at the atomic level. One technique, the analysis of relaxation dispersion phenomenon, is highly suited for studying the kinetics and thermodynamics of biological processes. Built on top of the relax computational environment for NMR dynamics is a new dispersion analysis designed to be comprehensive, accurate and easy-to-use. The software supports more models, both numeric and analytic, than current solutions. An automated protocol, available for scripting and driving the graphical user interface (GUI), is designed to simplify the analysis of dispersion data for NMR spectroscopists. Decreases in optimization time are granted by parallelization for running on computer clusters and by skipping an initial grid search by using parameters from one solution as the starting point for another —using analytic model results for the numeric models, taking advantage of model nesting, and using averaged non-clustered results for the clustered analysis.","lang":"eng"}],"publication_status":"published","volume":30,"title":"Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data","citation":{"short":"S. Morin, T.E. Linnet, M. Lescanne, P. Schanda, G.S. Thompson, M. Tollinger, K. Teilum, S. Gagné, D. Marion, C. Griesinger, M. Blackledge, E.J. d’Auvergne, Bioinformatics 30 (2014) 2219–2220.","ama":"Morin S, Linnet TE, Lescanne M, et al. Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. <i>Bioinformatics</i>. 2014;30(15):2219-2220. doi:<a href=\"https://doi.org/10.1093/bioinformatics/btu166\">10.1093/bioinformatics/btu166</a>","apa":"Morin, S., Linnet, T. E., Lescanne, M., Schanda, P., Thompson, G. S., Tollinger, M., … d’Auvergne, E. J. (2014). Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. <i>Bioinformatics</i>. Oxford University Press. <a href=\"https://doi.org/10.1093/bioinformatics/btu166\">https://doi.org/10.1093/bioinformatics/btu166</a>","chicago":"Morin, Sébastien, Troels E Linnet, Mathilde Lescanne, Paul Schanda, Gary S Thompson, Martin Tollinger, Kaare Teilum, et al. “Relax: The Analysis of Biomolecular Kinetics and Thermodynamics Using NMR Relaxation Dispersion Data.” <i>Bioinformatics</i>. Oxford University Press, 2014. <a href=\"https://doi.org/10.1093/bioinformatics/btu166\">https://doi.org/10.1093/bioinformatics/btu166</a>.","ieee":"S. Morin <i>et al.</i>, “Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data,” <i>Bioinformatics</i>, vol. 30, no. 15. Oxford University Press, pp. 2219–2220, 2014.","ista":"Morin S, Linnet TE, Lescanne M, Schanda P, Thompson GS, Tollinger M, Teilum K, Gagné S, Marion D, Griesinger C, Blackledge M, d’Auvergne EJ. 2014. Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. Bioinformatics. 30(15), 2219–2220.","mla":"Morin, Sébastien, et al. “Relax: The Analysis of Biomolecular Kinetics and Thermodynamics Using NMR Relaxation Dispersion Data.” <i>Bioinformatics</i>, vol. 30, no. 15, Oxford University Press, 2014, pp. 2219–20, doi:<a href=\"https://doi.org/10.1093/bioinformatics/btu166\">10.1093/bioinformatics/btu166</a>."},"author":[{"first_name":"Sébastien","full_name":"Morin, Sébastien","last_name":"Morin"},{"full_name":"Linnet, Troels E","first_name":"Troels E","last_name":"Linnet"},{"full_name":"Lescanne, Mathilde","first_name":"Mathilde","last_name":"Lescanne"},{"first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"last_name":"Thompson","first_name":"Gary S","full_name":"Thompson, Gary S"},{"full_name":"Tollinger, Martin","first_name":"Martin","last_name":"Tollinger"},{"first_name":"Kaare","full_name":"Teilum, Kaare","last_name":"Teilum"},{"full_name":"Gagné, Stéphane","first_name":"Stéphane","last_name":"Gagné"},{"full_name":"Marion, Dominique","first_name":"Dominique","last_name":"Marion"},{"first_name":"Christian","full_name":"Griesinger, Christian","last_name":"Griesinger"},{"last_name":"Blackledge","first_name":"Martin","full_name":"Blackledge, Martin"},{"first_name":"Edward J","full_name":"d’Auvergne, Edward J","last_name":"d’Auvergne"}],"type":"journal_article","day":"01","related_material":{"link":[{"url":"https://doi.org/10.1093/bioinformatics/btz397","relation":"erratum"}]},"doi":"10.1093/bioinformatics/btu166","language":[{"iso":"eng"}],"keyword":["Statistics and Probability","Computational Theory and Mathematics","Biochemistry","Molecular Biology","Computational Mathematics","Computer Science Applications"],"page":"2219-2220","date_created":"2020-09-18T10:08:07Z","extern":"1","month":"08","publisher":"Oxford University Press","status":"public","intvolume":"        30","quality_controlled":"1","publication":"Bioinformatics"},{"year":"2014","oa_version":"None","article_type":"original","publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"date_updated":"2023-08-08T07:25:37Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"pmid":["25072292"]},"scopus_import":"1","date_published":"2014-08-13T00:00:00Z","_id":"13401","abstract":[{"lang":"eng","text":"A compound combining the features of a molecular rotor and a photoswitch was synthesized and was shown to exist as three diastereomers, which interconvert via a reversible cyclic reaction scheme. Each of the three diastereomers was isolated, and by following the equilibration kinetics, activation barriers for all reactions were calculated. The results indicate that the properties of molecular switches depend heavily on their immediate chemical environment. The conclusions are important in the context of designing new switchable molecules and materials."}],"issue":"32","article_processing_charge":"No","volume":136,"publication_status":"published","author":[{"first_name":"Pintu K.","full_name":"Kundu, Pintu K.","last_name":"Kundu"},{"first_name":"Avishai","full_name":"Lerner, Avishai","last_name":"Lerner"},{"first_name":"Kristina","full_name":"Kučanda, Kristina","last_name":"Kučanda"},{"last_name":"Leitus","first_name":"Gregory","full_name":"Leitus, Gregory"},{"first_name":"Rafal","full_name":"Klajn, Rafal","last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"type":"journal_article","day":"13","title":"Cyclic kinetics during thermal equilibration of an axially chiral bis-spiropyran","citation":{"short":"P.K. Kundu, A. Lerner, K. Kučanda, G. Leitus, R. Klajn, Journal of the American Chemical Society 136 (2014) 11276–11279.","apa":"Kundu, P. K., Lerner, A., Kučanda, K., Leitus, G., &#38; Klajn, R. (2014). Cyclic kinetics during thermal equilibration of an axially chiral bis-spiropyran. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja505948q\">https://doi.org/10.1021/ja505948q</a>","ama":"Kundu PK, Lerner A, Kučanda K, Leitus G, Klajn R. Cyclic kinetics during thermal equilibration of an axially chiral bis-spiropyran. <i>Journal of the American Chemical Society</i>. 2014;136(32):11276-11279. doi:<a href=\"https://doi.org/10.1021/ja505948q\">10.1021/ja505948q</a>","ieee":"P. K. Kundu, A. Lerner, K. Kučanda, G. Leitus, and R. Klajn, “Cyclic kinetics during thermal equilibration of an axially chiral bis-spiropyran,” <i>Journal of the American Chemical Society</i>, vol. 136, no. 32. American Chemical Society, pp. 11276–11279, 2014.","ista":"Kundu PK, Lerner A, Kučanda K, Leitus G, Klajn R. 2014. Cyclic kinetics during thermal equilibration of an axially chiral bis-spiropyran. Journal of the American Chemical Society. 136(32), 11276–11279.","chicago":"Kundu, Pintu K., Avishai Lerner, Kristina Kučanda, Gregory Leitus, and Rafal Klajn. “Cyclic Kinetics during Thermal Equilibration of an Axially Chiral Bis-Spiropyran.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2014. <a href=\"https://doi.org/10.1021/ja505948q\">https://doi.org/10.1021/ja505948q</a>.","mla":"Kundu, Pintu K., et al. “Cyclic Kinetics during Thermal Equilibration of an Axially Chiral Bis-Spiropyran.” <i>Journal of the American Chemical Society</i>, vol. 136, no. 32, American Chemical Society, 2014, pp. 11276–79, doi:<a href=\"https://doi.org/10.1021/ja505948q\">10.1021/ja505948q</a>."},"doi":"10.1021/ja505948q","language":[{"iso":"eng"}],"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"pmid":1,"date_created":"2023-08-01T09:46:12Z","extern":"1","month":"08","page":"11276-11279","status":"public","intvolume":"       136","quality_controlled":"1","publication":"Journal of the American Chemical Society","publisher":"American Chemical Society"},{"citation":{"short":"P.K. Kundu, G.L. Olsen, V. Kiss, R. Klajn, Nature Communications 5 (2014).","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>","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>","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.","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.","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>."},"title":"Nanoporous frameworks exhibiting multiple stimuli responsiveness","day":"07","author":[{"full_name":"Kundu, Pintu K.","first_name":"Pintu K.","last_name":"Kundu"},{"first_name":"Gregory L.","full_name":"Olsen, Gregory L.","last_name":"Olsen"},{"first_name":"Vladimir","full_name":"Kiss, Vladimir","last_name":"Kiss"},{"first_name":"Rafal","full_name":"Klajn, Rafal","last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"type":"journal_article","pmid":1,"language":[{"iso":"eng"}],"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"doi":"10.1038/ncomms4588","extern":"1","month":"04","date_created":"2023-08-01T09:46:27Z","publisher":"Springer Nature","quality_controlled":"1","publication":"Nature Communications","status":"public","intvolume":"         5","article_type":"original","oa_version":"Published Version","year":"2014","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2023-08-08T07:28:10Z","scopus_import":"1","external_id":{"pmid":["24709950"]},"publication_identifier":{"eissn":["2041-1723"]},"article_processing_charge":"No","article_number":"3588","_id":"13402","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"}],"date_published":"2014-04-07T00:00:00Z","publication_status":"published","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms4588"}],"oa":1,"volume":5},{"publisher":"American Chemical Society","status":"public","intvolume":"       136","quality_controlled":"1","publication":"Journal of the American Chemical Society","page":"2711-2714","date_created":"2023-08-01T09:46:44Z","extern":"1","month":"02","pmid":1,"doi":"10.1021/ja411573a","language":[{"iso":"eng"}],"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"title":"Support curvature and conformational freedom control chemical reactivity of immobilized species","citation":{"mla":"Zdobinsky, Tino, et al. “Support Curvature and Conformational Freedom Control Chemical Reactivity of Immobilized Species.” <i>Journal of the American Chemical Society</i>, vol. 136, no. 7, American Chemical Society, 2014, pp. 2711–14, doi:<a href=\"https://doi.org/10.1021/ja411573a\">10.1021/ja411573a</a>.","ista":"Zdobinsky T, Sankar Maiti P, Klajn R. 2014. Support curvature and conformational freedom control chemical reactivity of immobilized species. Journal of the American Chemical Society. 136(7), 2711–2714.","ieee":"T. Zdobinsky, P. Sankar Maiti, and R. Klajn, “Support curvature and conformational freedom control chemical reactivity of immobilized species,” <i>Journal of the American Chemical Society</i>, vol. 136, no. 7. American Chemical Society, pp. 2711–2714, 2014.","chicago":"Zdobinsky, Tino, Pradipta Sankar Maiti, and Rafal Klajn. “Support Curvature and Conformational Freedom Control Chemical Reactivity of Immobilized Species.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2014. <a href=\"https://doi.org/10.1021/ja411573a\">https://doi.org/10.1021/ja411573a</a>.","apa":"Zdobinsky, T., Sankar Maiti, P., &#38; Klajn, R. (2014). Support curvature and conformational freedom control chemical reactivity of immobilized species. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja411573a\">https://doi.org/10.1021/ja411573a</a>","ama":"Zdobinsky T, Sankar Maiti P, Klajn R. Support curvature and conformational freedom control chemical reactivity of immobilized species. <i>Journal of the American Chemical Society</i>. 2014;136(7):2711-2714. doi:<a href=\"https://doi.org/10.1021/ja411573a\">10.1021/ja411573a</a>","short":"T. Zdobinsky, P. Sankar Maiti, R. Klajn, Journal of the American Chemical Society 136 (2014) 2711–2714."},"author":[{"last_name":"Zdobinsky","first_name":"Tino","full_name":"Zdobinsky, Tino"},{"first_name":"Pradipta","full_name":"Sankar Maiti, Pradipta","last_name":"Sankar Maiti"},{"last_name":"Klajn","first_name":"Rafal","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"type":"journal_article","day":"19","publication_status":"published","volume":136,"issue":"7","article_processing_charge":"No","date_published":"2014-02-19T00:00:00Z","_id":"13403","abstract":[{"text":"We show that bimolecular reactions between species confined to the surfaces of nanoparticles can be manipulated by the nature of the linker, as well as by the curvature of the underlying particles.","lang":"eng"}],"publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"date_updated":"2023-08-08T07:32:11Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":"1","external_id":{"pmid":["24320557"]},"year":"2014","oa_version":"None","article_type":"original"}]