@article{SperberWelkePetazzietal.2019,
  author    = {Sperber, Hannah Sabeth and Welke, Robert-William and Petazzi, Roberto Arturo and Bergmann, Ronny and Schade, Matthias and Shai, Yechiel and Chiantia, Salvatore and Herrmann, Andreas and Schwarzer, Roland},
  title     = {Self-association and subcellular localization of Puumala hantavirus envelope proteins},
  series = {Scientific reports},
  volume    = {9},
  journal   = {Scientific reports},
  publisher = {Nature Publ. Group},
  address   = {London},
  issn      = {2045-2322},
  doi       = {10.1038/s41598-018-36879-y},
  pages     = {15},
  year      = {2019},
  abstract  = {Hantavirus assembly and budding are governed by the surface glycoproteins Gn and Gc. In this study, we investigated the glycoproteins of Puumala, the most abundant Hantavirus species in Europe, using fluorescently labeled wild-type constructs and cytoplasmic tail (CT) mutants. We analyzed their intracellular distribution, co-localization and oligomerization, applying comprehensive live, single-cell fluorescence techniques, including confocal microscopy, imaging flow cytometry, anisotropy imaging and Number\&Brightness analysis. We demonstrate that Gc is significantly enriched in the Golgi apparatus in absence of other viral components, while Gn is mainly restricted to the endoplasmic reticulum (ER). Importantly, upon co-expression both glycoproteins were found in the Golgi apparatus. Furthermore, we show that an intact CT of Gc is necessary for efficient Golgi localization, while the CT of Gn influences protein stability. Finally, we found that Gn assembles into higher-order homo-oligomers, mainly dimers and tetramers, in the ER while Gc was present as mixture of monomers and dimers within the Golgi apparatus. Our findings suggest that PUUV Gc is the driving factor of the targeting of Gc and Gn to the Golgi region, while Gn possesses a significantly stronger self-association potential.},
  language  = {en}
}
@article{Schade2011,
  author    = {Schade, Robert},
  title     = {Flammende Prospekte : die Großstadt als Bewußtseinspiel und die Ambivalenz des untergeordneten Raums : Andrej Belyis Petersburg},
  isbn      = {978-3-8376-1404-6},
  year      = {2011},
  language  = {de}
}
@phdthesis{Schade2017,
  author    = {Schade, Robert},
  title     = {Schwankende Ansichten},
  series = {Metabasis - Transkriptionen zwischen Literaturen, K{\"u}nsten und Medien ; 19},
  journal   = {Metabasis - Transkriptionen zwischen Literaturen, K{\"u}nsten und Medien ; 19},
  publisher = {transcript},
  address   = {Bielefeld},
  isbn      = {978-3-8376-3993-3},
  school      = {Universit{\"a}t Potsdam},
  pages     = {242},
  year      = {2017},
  abstract  = {Neu sehen, anders sehen - seit dem 19. Jahrhundert hat sich in der Literatur eine {\"A}sthetik alternativer Sehformen etabliert, die die eigene Wahrnehmung zunehmend infrage stellt und sich in der Figur des Schwankens manifestiert. Robert Schade er{\"o}ffnet einen Einblick in die Geschichte dieser alternativen Sehformen, indem er ausgehend von {\"o}konomischen Wahrnehmungstheorien des 19. und 20. Jahrhunderts Fragestellungen aus Psychologie, Philosophie und {\"A}sthetik verfolgt. Er stellt auf diesem Wege erstmals eine Verbindung zwischen der Sehtheorie Hermann von Helmholtz' und der Verfremdungs{\"a}sthetik Viktor Shklovskijs her. Am Beispiel von vier Werkuntersuchungen (von Gustave Caillebotte, Andrej Belyj, H.G. Wells und Luigi Pirandello) werden die Vernetztheit und das kritische Potenzial der Figur des Schwankens in unterschiedlichen Diskursen illustriert.},
  language  = {de}
}
@misc{SperberWelkePetazzietal.2019,
  author    = {Sperber, Hannah Sabeth and Welke, Robert-William and Petazzi, Roberto Arturo and Bergmann, Ronny and Schade, Matthias and Shai, Yechiel and Chiantia, Salvatore and Herrmann, Andreas and Schwarzer, Roland},
  title     = {Self-association and subcellular localization of Puumala hantavirus envelope proteins},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {648},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-42504},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-425040},
  pages     = {15},
  year      = {2019},
  abstract  = {Hantavirus assembly and budding are governed by the surface glycoproteins Gn and Gc. In this study, we investigated the glycoproteins of Puumala, the most abundant Hantavirus species in Europe, using fluorescently labeled wild-type constructs and cytoplasmic tail (CT) mutants. We analyzed their intracellular distribution, co-localization and oligomerization, applying comprehensive live, single-cell fluorescence techniques, including confocal microscopy, imaging flow cytometry, anisotropy imaging and Number\&Brightness analysis. We demonstrate that Gc is significantly enriched in the Golgi apparatus in absence of other viral components, while Gn is mainly restricted to the endoplasmic reticulum (ER). Importantly, upon co-expression both glycoproteins were found in the Golgi apparatus. Furthermore, we show that an intact CT of Gc is necessary for efficient Golgi localization, while the CT of Gn influences protein stability. Finally, we found that Gn assembles into higher-order homo-oligomers, mainly dimers and tetramers, in the ER while Gc was present as mixture of monomers and dimers within the Golgi apparatus. Our findings suggest that PUUV Gc is the driving factor of the targeting of Gc and Gn to the Golgi region, while Gn possesses a significantly stronger self-association potential.},
  language  = {en}
}
@incollection{Schade2017,
  author    = {Schade, Robert},
  title     = {Bizarrerie als Verfahren},
  series = {Visualisierung, Visibilisierung und Verschriftlichung},
  booktitle = {Visualisierung, Visibilisierung und Verschriftlichung},
  publisher = {Tranvia},
  address   = {Berlin},
  isbn      = {978-3-938944-93-6},
  publisher      = {Universit{\"a}t Potsdam},
  pages     = {341 -- 353},
  year      = {2017},
  language  = {de}
}