@article{SchulzErleGraefetal.2009,
  author    = {Schulz, Irene and Erle, Alexander and Gr{\"a}f, Ralph and Krueger, Anne and Lohmeier, Heiner and Putzler, Sascha and Samereier, Matthias and Weidenthaler, Sebastian},
  title     = {Identification and cell cycle-dependent localization of nine novel, genuine centrosomal components in Dictyostelium discoideum},
  issn      = {0886-1544},
  doi       = {10.1002/Cm.20384},
  year      = {2009},
  abstract  = {The centrosome is the main microtubule-organizing center and constitutes the largest protein complex in a eukaryotic cell. The Dictyostelium centrosome is an established model for acentriolar centrosomes and it consists of a layered core structure Surrounded by a so-called corona, which harbors microtubule nucleation complexes. We have identified 34 new centrosomal candidate proteins through mass spectrometrical analysis of the proteome of isolated Dictyostelium centrosomes. Here we present a characterization of 12 centrosomal candidate proteins all featuring coiled coil regions and low expression levels, which are the most common attributes of centrosomal proteins. We used GFP fusion proteins to localize the candidate proteins in whole cells and on microtubule-free, isolated centrosomes. Thus we were able to identify nine new genuine centrosomal proteins including a putative orthologue of Cep192, an interaction partner of polo-like kinase 4 in human centriole biogenesis. In this respect, centrosomal localization of the only polo-like kinase in Dictyostelium, Pik, is also shown in this work. Using confocal deconvolution microscopy, four components, CP39, CP55, CP75, and CP91 could be clearly assigned to the so far almost uncharacterized centrosomal core structure, while CP148 and Cep192 localized to a zone between that of corona marker and core proteins. Finally, CP103 and CP248 were constituents of the corona. In contrast, NE81 was localized at the nuclear envelope and three others, an orthologue of the spindle checkpoint component Mad1, the novel Cenp68, and the centrosomal CP248 were observed at the centromeres, which are clustered and linked to the centrosome throughout the entire cell cycle. Cell Motil. Cytoskeleton 66: 915-928, 2009.},
  language  = {en}
}
@article{SchulzBaumannSamereieretal.2009,
  author    = {Schulz, Irene and Baumann, Otto and Samereier, Matthias and Zoglmeier, Christine and Gr{\"a}f, Ralph},
  title     = {Dictyostelium Sun1 is a dynamic membrane protein of both nuclear membranes and required for centrosomal association with clustered centromeres},
  issn      = {0171-9335},
  doi       = {10.1016/j.ejcb.2009.06.003},
  year      = {2009},
  abstract  = {Centrosomal attachment to nuclei is crucial for proper mitosis and nuclear positioning in various organisms, and generally involves Sun-family proteins located at the inner nuclear envelope. There is still no common scheme for the outer nuclear membrane proteins interacting with Sun I in centrosome/nucleus attachment. Here we propose a model in which Sun1 mediates a physical link between centrosomes and clustered centromeres through both nuclear membranes in Dictyostelium. For the first time we provide a detailed microscopic analysis of the centrosomal and nuclear envelope localization of endogenous Dictyostelium Sun1 during interphase and mitosis. By immunogold electron microscopy we show that Sun1 is a resident of both nuclear membranes. Disruption of Sun1 function by overexpression of full-length GFP-Sun1 or a GFP-Sun-domain deletion construct revealed not only the established function in centrosome/nucleus attachment and maintenance of ploidy, but also a requirement of Sun1 for the association of the centromere cluster with the centrosome. Live-cell imaging visualized the occurrence of mitotic defects, and demonstrated the requirement of microtubules for dynamic distance changes between centrosomes and nuclei. FRAP analysis revealed at least two populations of Sun1, with an immobile fraction associated with the centrosome, and a mobile fraction in the nuclear envelope.},
  language  = {en}
}
@article{SchulzErleGraefetal.2009,
  author    = {Schulz, Irene and Erle, Alexander and Gr{\"a}f, Ralph and Krueger, Anne and Putzler, Sascha and Samereier, Matthias and Weidenthaler, Sebastian},
  title     = {Cell cycle-dependent localization of novel centrosomal and centromeric proteins in Dictyostelium},
  issn      = {0171-9335},
  doi       = {10.1016/S0171-9335(09)00023-5},
  year      = {2009},
  language  = {en}
}
@book{RanaMohapatraSidorovaetal.2022,
  author    = {Rana, Kaushik and Mohapatra, Durga Prasad and Sidorova, Julia and Lundberg, Lars and Sk{\"o}ld, Lars and Lopes Grim, Lu{\´i}s Fernando and Sampaio Gradvohl, Andr{\´e} Leon and Cremerius, Jonas and Siegert, Simon and Weltzien, Anton von and Baldi, Annika and Klessascheck, Finn and Kalancha, Svitlana and Lichtenstein, Tom and Shaabani, Nuhad and Meinel, Christoph and Friedrich, Tobias and Lenzner, Pascal and Schumann, David and Wiese, Ingmar and Sarna, Nicole and Wiese, Lena and Tashkandi, Araek Sami and van der Walt, Est{\´e}e and Eloff, Jan H. P. and Schmidt, Christopher and H{\"u}gle, Johannes and Horschig, Siegfried and Uflacker, Matthias and Najafi, Pejman and Sapegin, Andrey and Cheng, Feng and Stojanovic, Dragan and Stojnev Ilić, Aleksandra and Djordjevic, Igor and Stojanovic, Natalija and Predic, Bratislav and Gonz{\´a}lez-Jim{\´e}nez, Mario and de Lara, Juan and Mischkewitz, Sven and Kainz, Bernhard and van Hoorn, Andr{\´e} and Ferme, Vincenzo and Schulz, Henning and Knigge, Marlene and Hecht, Sonja and Prifti, Loina and Krcmar, Helmut and Fabian, Benjamin and Ermakova, Tatiana and Kelkel, Stefan and Baumann, Annika and Morgenstern, Laura and Plauth, Max and Eberhard, Felix and Wolff, Felix and Polze, Andreas and Cech, Tim and Danz, Noel and Noack, Nele Sina and Pirl, Lukas and Beilharz, Jossekin Jakob and De Oliveira, Roberto C. L. and Soares, F{\´a}bio Mendes and Juiz, Carlos and Bermejo, Belen and M{\"u}hle, Alexander and Gr{\"u}ner, Andreas and Saxena, Vageesh and Gayvoronskaya, Tatiana and Weyand, Christopher and Krause, Mirko and Frank, Markus and Bischoff, Sebastian and Behrens, Freya and R{\"u}ckin, Julius and Ziegler, Adrian and Vogel, Thomas and Tran, Chinh and Moser, Irene and Grunske, Lars and Sz{\´a}rnyas, G{\´a}bor and Marton, J{\´o}zsef and Maginecz, J{\´a}nos and Varr{\´o}, D{\´a}niel and Antal, J{\´a}nos Benjamin},
  title     = {HPI Future SOC Lab - Proceedings 2018},
  number    = {151},
  editor    = {Meinel, Christoph and Polze, Andreas and Beins, Karsten and Strotmann, Rolf and Seibold, Ulrich and R{\"o}dszus, Kurt and M{\"u}ller, J{\"u}rgen},
  publisher = {Universit{\"a}tsverlag Potsdam},
  address   = {Potsdam},
  isbn      = {978-3-86956-547-7},
  issn      = {1613-5652},
  doi       = {10.25932/publishup-56371},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-563712},
  publisher      = {Universit{\"a}t Potsdam},
  pages     = {x, 277},
  year      = {2022},
  abstract  = {The "HPI Future SOC Lab" is a cooperation of the Hasso Plattner Institute (HPI) and industry partners. Its mission is to enable and promote exchange and interaction between the research community and the industry partners. The HPI Future SOC Lab provides researchers with free of charge access to a complete infrastructure of state of the art hard and software. This infrastructure includes components, which might be too expensive for an ordinary research environment, such as servers with up to 64 cores and 2 TB main memory. The offerings address researchers particularly from but not limited to the areas of computer science and business information systems. Main areas of research include cloud computing, parallelization, and In-Memory technologies. This technical report presents results of research projects executed in 2018. Selected projects have presented their results on April 17th and November 14th 2017 at the Future SOC Lab Day events.},
  language  = {en}
}