@article{ParkKrauseKarnahletal.2018,
  author    = {Park, Misoon and Krause, Cornelia and Karnahl, Matthias and Reichardt, Ilka and El Kasmi, Farid and Mayer, Ulrike and Stierhof, York-Dieter and Hiller, Ulrike and Strompen, Georg and Bayer, Martin and Kientz, Marika and Sato, Masa H. and Nishimura, Marc T. and Dangl, Jeffery L. and Sanderfoot, Anton A. and J{\"u}rgens, Gerd},
  title     = {Concerted Action of Evolutionarily Ancient and Novel SNARE Complexes in Flowering-Plant Cytokinesis},
  series = {Developmental cell},
  volume    = {44},
  journal   = {Developmental cell},
  number    = {4},
  publisher = {Cell Press},
  address   = {Cambridge},
  issn      = {1534-5807},
  doi       = {10.1016/j.devcel.2017.12.027},
  pages     = {500 -- +},
  year      = {2018},
  abstract  = {Membrane vesicles delivered to the cell-division plane fuse with one another to form the partitioning membrane during plant cytokinesis, starting in the cell center. In Arabidopsis, this requires SNARE complexes involving the cytokinesis-specific Qa-SNARE KNOLLE. However, cytokinesis still occurs in knolle mutant embryos, suggesting contributions from KNOLLE-independent SNARE complexes. Here we show that Qa-SNARE SYP132, having counterparts in lower plants, functionally overlaps with the flowering plant-specific KNOLLE. SYP132 mutation causes cytokinesis defects, knolle syp132 double mutants consist of only one or a few multi-nucleate cells, and SYP132 has the same SNARE partners as KNOLLE. SYP132 and KNOLLE also have non-overlapping functions in secretion and in cellularization of the embryo-nourishing endosperm resulting from double fertilization unique to flowering plants. Evolutionarily ancient non-specialized SNARE complexes originating in algae were thus amended by the appearance of cytokinesis-specific SNARE complexes, meeting the high demand for membrane-fusion capacity during endosperm cellularization in angiosperms.},
  language  = {en}
}
@article{FrescatadaRosaStanislasBackuesetal.2014,
  author    = {Frescatada-Rosa, Marcia and Stanislas, Thomas and Backues, Steven K. and Reichardt, Ilka and Men, Shuzhen and Boutte, Yohann and Juergens, Gerd and Moritz, Thomas and Bednarek, Sebastian York and Grebe, Markus},
  title     = {High lipid order of Arabidopsis cell-plate membranes mediated by sterol and Dynamin-Related Protein 1A function},
  series = {The plant journal},
  volume    = {80},
  journal   = {The plant journal},
  number    = {5},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {0960-7412},
  doi       = {10.1111/tpj.12674},
  pages     = {745 -- 757},
  year      = {2014},
  abstract  = {Membranes of eukaryotic cells contain high lipid-order sterol-rich domains that are thought to mediate temporal and spatial organization of cellular processes. Sterols are crucial for execution of cytokinesis, the last stage of cell division, in diverse eukaryotes. The cell plate of higher-plant cells is the membrane structure that separates daughter cells during somatic cytokinesis. Cell-plate formation in Arabidopsis relies on sterol- and DYNAMIN-RELATED PROTEIN1A (DRP1A)-dependent endocytosis. However, functional relationships between lipid membrane order or lipid packing and endocytic machinery components during eukaryotic cytokinesis have not been elucidated. Using ratiometric live imaging of lipid order-sensitive fluorescent probes, we show that the cell plate of Arabidopsis thaliana represents a dynamic, high lipid-order membrane domain. The cell-plate lipid order was found to be sensitive to pharmacological and genetic alterations of sterol composition. Sterols co-localize with DRP1A at the cell plate, and DRP1A accumulates in detergent-resistant membrane fractions. Modifications of sterol concentration or composition reduce cell-plate membrane order and affect DRP1A localization. Strikingly, DRP1A function itself is essential for high lipid order at the cell plate. Our findings provide evidence that the cell plate represents a high lipid-order domain, and pave the way to explore potential feedback between lipid order and function of dynamin-related proteins during cytokinesis.},
  language  = {en}
}
@article{KaneHoffmannBaumgaerteletal.2008,
  author    = {Kane, Avinash S. and Hoffmann, Armin S. and Baumg{\"a}rtel, Peter and Seckler, Robert and Reichardt, Gerd and Horsley, David A. and Schuler, Benjamin and Bakajin, Olgica},
  title     = {Microfluidic mixers for the investigation of rapid protein folding kinetics using synchrotron radiation circular dichroism spectroscopy},
  issn      = {0003-2700},
  year      = {2008},
  abstract  = {We have developed a microfluidic mixer optimized for rapid measurements of protein folding kinetics using synchrotron radiation circular dichroism (SRCD) spectroscopy. The combination of fabrication in fused silica and synchrotron radiation allows measurements at wavelengths below 220 nm, the typical limit of commercial instrumentation. At these wavelengths, the discrimination between the different types of protein secondary structure increases sharply. The device was optimized for rapid mixing at moderate sample consumption by employing a serpentine channel design, resulting in a dead time of less than 200 ;s. Here, we discuss the design and fabrication of the mixer and quantify the mixing efficiency using wide-field and confocal epi-fluorescence microscopy. We demonstrate the performance of the device in SRCD measurements of the folding kinetics of cytochrome c, a small, fast-folding protein. Our results show that the combination of SRCD with microfluidic mixing opens new possibilities for investigating rapid conformational changes in biological macromolecules that have previously been inaccessible.},
  language  = {en}
}
@misc{AbramowskiAharonianBenkhalietal.2015,
  author    = {Abramowski, Attila and Aharonian, Felix A. and Benkhali, Faical Ait and Akhperjanian, A. G. and Ang{\"u}ner, Ekrem Oǧuzhan and Backes, Michael and Balenderan, Shangkari and Balzer, Arnim and Barnacka, Anna and Becherini, Yvonne and Tjus, Julia Becker and Berge, David and Bernhard, Sabrina and Bernl{\"o}hr, Konrad and Birsin, E. and Biteau, Jonathan and B{\"o}ttcher, Markus and Boisson, Catherine and Bolmont, J. and Bordas, Pol and Bregeon, Johan and Brun, Francois and Brun, Pierre and Bryan, Mark and Bulik, Tomasz and Carrigan, Svenja and Casanova, Sabrina and Chadwick, Paula M. and Chakraborty, Nachiketa and Chalme-Calvet, R. and Chaves, Ryan C. G. and Chretien, M. and Colafrancesco, Sergio and Cologna, Gabriele and Conrad, Jan and Couturier, Claire and Cui, Yudong and Davids, Isak Delberth and Degrange, Bernhard and Deil, Christoph and deWilt, P. and Djannati-Ata{\"i}, A. and Domainko, Wilfried and Donath, Axel and Dubus, G. and Dutson, K. and Dyks, J. and Dyrda, M. and Edwards, Tanya and Egberts, Kathrin and Eger, Peter and Espigat, P. and Farnier, C. and Fegan, Stephen and Feinstein, Fabrice and Fernandes, Milton Virgilio and Fernandez, Diane and Fiasson, A. and Fontaine, Gerard and F{\"o}rster, Andreas and Fuessling, M. and Gabici, S. and Gajdus, M. and Gallant, Yves A. and Garrigoux, Tania and Giavitto, G. and Giebels, Berrie and Glicenstein, Jean-Francois and Gottschall, Daniel and Grondin, M. -H. and Grudzinska, M. and Hadasch, Daniela and Haeffner, S. and Hahn, Joachim and Harris, Jonathan and Heinzelmann, G{\"o}tz and Henri, G. and Hermann, German and Hervet, O. and Hillert, Andreas and Hinton, James Anthony and Hofmann, Werner and Hofverberg, Petter and Holler, Markus and Horns, Dieter and Ivascenko, Alex and Jacholkowska, A. and Jahn, C. and Jamrozy, Marek and Janiak, M. and Jankowsky, F. and Jung-Richardt, I. and Kastendieck, Max Anton and Katarzynski, K. and Katz, U. and Kaufmann, S. and Khelifi, B. and Kieffer, Michel and Klepser, S. and Klochkov, Dmitry and Kluzniak, W. and Kolitzus, David and Komin, Nu and Kosack, Karl and Krakau, Steffen and Krayzel, F. and Krueger, Pat P. and Laffon, H. and Lamanna, G. and Lefaucheur, J. and Lefranc, Valentin and Lemiere, A. and Lemoine-Goumard, M. and Lenain, J. -P. and Lohse, Thomas and Lopatin, A. and Lu, Chia-Chun and Marandon, Vincent and Marcowith, Alexandre and Marx, Ramin and Maurin, G. and Maxted, Nigel and Mayer, Michael and McComb, T. J. Lowry and Mehault, J. and Meintjes, P. J. and Menzler, Ulf and Meyer, M. and Mitchell, Alison M. W. and Moderski, R. and Mohamed, M. and Mora, K. and Moulin, Emmanuel and Murach, Thomas and de Naurois, Mathieu and Niemiec, J. and Nolan, Sam J. and Oakes, Louise and Odaka, Hirokazu and Ohm, S. and Optiz, Bj{\"o}rn and Ostrowski, Michal and Oya, I. and Panter, Michael and Parsons, R. Daniel and Arribas, M. Paz and Pekeur, Nikki W. and Pelletier, G. and Petrucci, P. -O. and Peyaud, B. and Pita, S. and Poon, Helen and P{\"u}hlhofer, Gerd and Punch, M. and Quirrenbach, A. and Raab, S. and Reichardt, I. and Reimer, Anita and Reimer, Olaf and Renaud, Metz and de los Reyes, Raquel and Rieger, Frank and Romoli, C. and Rosier-Lees, S. and Rowell, G. and Rudak, B. and Rulten, C. B. and Sahakian, Vardan and Salek, D. and Sanchez, David M. and Santangelo, Andrea and Schlickeiser, Reinhard and Schuessler, F. and Schulz, A. and Schwanke, Ullrich and Schwarzburg, S. and Schwemmer, S. and Sol, H. and Spanier, Felix and Spengler, G. and Spies, Franziska and Stawarz, Lukasz and Steenkamp, Riaan and Stegmann, Christian and Stinzing, F. and Stycz, K. and Sushch, Iurii and Tavernet, J. -P. and Tavernier, T. and Taylor, A. M. and Terrier, R. and Tluczykont, Martin and Trichard, C. and Valerius, K. and van Eldik, C. and van Soelen, B. and Vasileiadis, Georges and Veh, J. and Venter, Christo and Viana, Aion and Vincent, P. and Vink, Jacco and V{\"o}lk, Heinrich J. and Volpe, Francesca and Vorster, Martine and Vuillaume, T. and Wagner, S. J. and Wagner, P. and Wagner, R. M. and Ward, Martin and Weidinger, Matthias and Weitzel, Quirin and White, R. and Wierzcholska, A. and Willmann, P. and Woernlein, A. and Wouters, D. and Yang, Ruizhi and Zabalza, Victor and Zaborov, Dmitry and Zacharias, M. and Zdziarski, A. A. and Zech, Alraune and Zechlin, Hannes -S.},
  title     = {H.E.S.S. detection of TeV emission from the interaction region between the supernova remnant G349.7+0.2 and a molecular cloud (vol 574, A100, 2015)},
  series = {Astronomy and astrophysics : an international weekly journal},
  volume    = {580},
  journal   = {Astronomy and astrophysics : an international weekly journal},
  publisher = {EDP Sciences},
  address   = {Les Ulis},
  organization    = {HESS Collaboration},
  issn      = {1432-0746},
  doi       = {10.1051/0004-6361/201425070e},
  pages     = {2},
  year      = {2015},
  language  = {en}
}
@article{HoffmannKaneNettelsetal.2007,
  author    = {Hoffmann, Armin S. and Kane, Avinash S. and Nettels, Daniel and Hertzog, David E. and Baumg{\"a}rtel, Peter and Lengefeld, Jan and Reichardt, Gerd and Horsley, David A. and Seckler, Robert and Bakajin, Olgica and Schuler, Benjamin},
  title     = {Mapping protein collapse with single molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy},
  issn      = {0027-8424},
  year      = {2007},
  language  = {en}
}